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Colicin - Wikipedia

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href="https://it.wikipedia.org/wiki/Colicina_E3" title="Colicina E3 – Italian" lang="it" hreflang="it" data-title="Colicina E3" data-language-autonym="Italiano" data-language-local-name="Italian" class="interlanguage-link-target"><span>Italiano</span></a></li><li class="interlanguage-link interwiki-nl mw-list-item"><a href="https://nl.wikipedia.org/wiki/Colicine" title="Colicine – Dutch" lang="nl" hreflang="nl" data-title="Colicine" data-language-autonym="Nederlands" data-language-local-name="Dutch" class="interlanguage-link-target"><span>Nederlands</span></a></li><li class="interlanguage-link interwiki-sk mw-list-item"><a href="https://sk.wikipedia.org/wiki/Kolic%C3%ADn" title="Kolicín – Slovak" lang="sk" hreflang="sk" data-title="Kolicín" data-language-autonym="Slovenčina" data-language-local-name="Slovak" class="interlanguage-link-target"><span>Slovenčina</span></a></li> </ul> <div class="after-portlet after-portlet-lang"><span class="wb-langlinks-edit wb-langlinks-link"><a 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dir="ltr"><div class="shortdescription nomobile noexcerpt noprint searchaux" style="display:none">Type of bacteriocin produced by and toxic to some strains of Escherichia coli</div> <style data-mw-deduplicate="TemplateStyles:r1236090951">.mw-parser-output .hatnote{font-style:italic}.mw-parser-output div.hatnote{padding-left:1.6em;margin-bottom:0.5em}.mw-parser-output .hatnote i{font-style:normal}.mw-parser-output .hatnote+link+.hatnote{margin-top:-0.5em}@media print{body.ns-0 .mw-parser-output .hatnote{display:none!important}}</style><div role="note" class="hatnote navigation-not-searchable">Not to be confused with <a href="/wiki/Colchicine" title="Colchicine">Colchicine</a>.</div><style data-mw-deduplicate="TemplateStyles:r1257001546">.mw-parser-output .infobox-subbox{padding:0;border:none;margin:-3px;width:auto;min-width:100%;font-size:100%;clear:none;float:none;background-color:transparent}.mw-parser-output .infobox-3cols-child{margin:auto}.mw-parser-output .infobox .navbar{font-size:100%}@media screen{html.skin-theme-clientpref-night .mw-parser-output .infobox-full-data:not(.notheme)>div:not(.notheme)[style]{background:#1f1f23!important;color:#f8f9fa}}@media screen and (prefers-color-scheme:dark){html.skin-theme-clientpref-os .mw-parser-output .infobox-full-data:not(.notheme) div:not(.notheme){background:#1f1f23!important;color:#f8f9fa}}@media(min-width:640px){body.skin--responsive .mw-parser-output .infobox-table{display:table!important}body.skin--responsive .mw-parser-output .infobox-table>caption{display:table-caption!important}body.skin--responsive .mw-parser-output .infobox-table>tbody{display:table-row-group}body.skin--responsive .mw-parser-output .infobox-table tr{display:table-row!important}body.skin--responsive .mw-parser-output .infobox-table th,body.skin--responsive .mw-parser-output .infobox-table td{padding-left:inherit;padding-right:inherit}}</style><table class="infobox"><tbody><tr><th colspan="2" class="infobox-above">Colicin</th></tr><tr><td colspan="2" class="infobox-image"><span class="mw-default-size" typeof="mw:File/Frameless"><a href="/wiki/File:PDB_2ivz_EBI.jpg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/e/e3/PDB_2ivz_EBI.jpg/220px-PDB_2ivz_EBI.jpg" decoding="async" width="220" height="165" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/e/e3/PDB_2ivz_EBI.jpg/330px-PDB_2ivz_EBI.jpg 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/e/e3/PDB_2ivz_EBI.jpg/440px-PDB_2ivz_EBI.jpg 2x" data-file-width="800" data-file-height="600" /></a></span><div class="infobox-caption">Structure of <a href="/wiki/TolB" class="mw-redirect" title="TolB">TolB</a> in complex with a peptide of the colicin e9 t-domain</div></td></tr><tr><th colspan="2" class="infobox-header" style="background-color: #ddd">Identifiers</th></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3">Symbol</th><td class="infobox-data" style="background-color: #eee">Colicin</td></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3"><a href="/wiki/Pfam" title="Pfam">Pfam</a></th><td class="infobox-data pfam" style="background-color: #eee"><a rel="nofollow" class="external text" href="https://www.ebi.ac.uk/interpro/entry/pfam/PF03515">PF03515</a></td></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3"><a href="/wiki/Pfam" title="Pfam">Pfam</a> clan</th><td class="infobox-data" style="background-color: #eee"><a rel="nofollow" class="external text" href="https://www.ebi.ac.uk/interpro/set/pfam/CL0446/">CL0446</a></td></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3"><a href="/wiki/InterPro" title="InterPro">InterPro</a></th><td class="infobox-data" style="background-color: #eee"><a rel="nofollow" class="external text" href="https://www.ebi.ac.uk/interpro/entry/IPR003058">IPR003058</a></td></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3"><a href="/wiki/Structural_Classification_of_Proteins" class="mw-redirect" title="Structural Classification of Proteins">SCOP2</a></th><td class="infobox-data" style="background-color: #eee"><a rel="nofollow" class="external text" href="http://scop2.mrc-lmb.cam.ac.uk/search?t=txt;q=1jch">1jch</a> / <a rel="nofollow" class="external text" href="https://scop.berkeley.edu/pdb/code=1jch">SCOPe</a> / <a rel="nofollow" class="external text" href="http://supfam.org/SUPERFAMILY/cgi-bin/search.cgi?search_field=1jch">SUPFAM</a></td></tr><tr><td colspan="2" class="infobox-full-data" style="background-color: #eee"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1257001546"><table class="infobox mw-collapsible mw-collapsed" style="float:none; clear:none; margin:0; border-width:0; border-collapse:collapse; text-align:left; width:100%"><tbody><tr><th colspan="2" class="infobox-header" style="background-color: #ddd">Available protein structures:</th></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3; border:#fafafa 2px solid; border-width:3px 2px 0 0;"><a href="/wiki/Pfam" title="Pfam">Pfam</a> &#160;</th><td class="infobox-data" style="background-color: #eee; border:#fafafa 2px solid; border-width:3px 0 0 2px;"><a rel="nofollow" class="external text" href="http://pfam.xfam.org/family/PF03515?tab=pdbBlock">structures</a> / <a rel="nofollow" class="external text" href="http://prodata.swmed.edu/ecod/complete/search?kw=PF03515">ECOD</a> &#160;</td></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3; border:#fafafa 2px solid; border-width:3px 2px 0 0;"><a href="/wiki/Protein_Data_Bank" title="Protein Data Bank">PDB</a></th><td class="infobox-data" style="background-color: #eee; border:#fafafa 2px solid; border-width:3px 0 0 2px;"><a rel="nofollow" class="external text" href="https://www.rcsb.org/search?q=rcsb_polymer_entity_annotation.annotation_id:PF03515%20AND%20rcsb_polymer_entity_annotation.type:Pfam">RCSB PDB</a>; <a rel="nofollow" class="external text" href="https://www.ebi.ac.uk/pdbe/entry/search/index?pfam_accession:PF03515">PDBe</a>; <a rel="nofollow" class="external text" href="https://pdbj.org/search/pdb?other_db_select=PFam&amp;other_db_field=PF03515">PDBj</a></td></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3; border:#fafafa 2px solid; border-width:3px 2px 0 0;"><a href="/wiki/PDBsum" title="PDBsum">PDBsum</a></th><td class="infobox-data" style="background-color: #eee; border:#fafafa 2px solid; border-width:3px 0 0 2px;"><a rel="nofollow" class="external text" href="https://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPfamStr.pl?pfam_id=PF03515">structure summary</a></td></tr></tbody></table></td></tr></tbody></table> <p>A <b>colicin</b> is a type of <a href="/wiki/Bacteriocin" title="Bacteriocin">bacteriocin</a> produced by and toxic to some strains of <i><a href="/wiki/Escherichia_coli" title="Escherichia coli">Escherichia coli</a></i>.<sup id="cite_ref-1" class="reference"><a href="#cite_note-1"><span class="cite-bracket">&#91;</span>1<span class="cite-bracket">&#93;</span></a></sup> Colicins are released into the environment to reduce competition from other <a href="/wiki/Bacterial_strain" class="mw-redirect" title="Bacterial strain">bacterial strains</a>. Colicins bind to <a href="/wiki/TonB-dependent_receptors" class="mw-redirect" title="TonB-dependent receptors">outer membrane receptors</a>, using them to <a href="/wiki/Translocase_of_the_outer_membrane" title="Translocase of the outer membrane">translocate</a> to the cytoplasm or cytoplasmic membrane, where they exert their cytotoxic effect, including depolarisation of the cytoplasmic membrane, <a href="/wiki/DNase" class="mw-redirect" title="DNase">DNase</a> activity, <a href="/wiki/RNase" class="mw-redirect" title="RNase">RNase</a> activity, or inhibition of <a href="/wiki/Murein" class="mw-redirect" title="Murein">murein</a> synthesis. </p> <meta property="mw:PageProp/toc" /> <div class="mw-heading mw-heading2"><h2 id="Structure">Structure</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Colicin&amp;action=edit&amp;section=1" title="Edit section: Structure"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Channel-forming colicins (colicins A, B, E1, Ia, Ib, and N) are <a href="/wiki/Transmembrane_protein" title="Transmembrane protein">transmembrane proteins</a> that depolarize the cytoplasmic membrane, leading to dissipation of cellular energy.<sup id="cite_ref-PUB00030669_2-0" class="reference"><a href="#cite_note-PUB00030669-2"><span class="cite-bracket">&#91;</span>2<span class="cite-bracket">&#93;</span></a></sup> These colicins contain at least three domains: an N-terminal translocation domain responsible for movement across the <a href="/wiki/Bacterial_outer_membrane" title="Bacterial outer membrane">outer membrane</a> and <a href="/wiki/Periplasmic_space" class="mw-redirect" title="Periplasmic space">periplasmic space</a> (T domain); a central domain responsible for receptor recognition (R domain); and a C-terminal <a href="/wiki/Cytotoxic" class="mw-redirect" title="Cytotoxic">cytotoxic</a> domain responsible for channel formation in the cytoplasmic membrane (C domain).<sup id="cite_ref-PUB00034705_3-0" class="reference"><a href="#cite_note-PUB00034705-3"><span class="cite-bracket">&#91;</span>3<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-4" class="reference"><a href="#cite_note-4"><span class="cite-bracket">&#91;</span>4<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-:0_5-0" class="reference"><a href="#cite_note-:0-5"><span class="cite-bracket">&#91;</span>5<span class="cite-bracket">&#93;</span></a></sup> R domain regulates the target and binds to the receptor on the sensitive cell. T domain is involved in translocation, co-opting the machinery of the target cell. The C domain is the 'killing' domain and may produce a pore in the target <a href="/wiki/Cell_membrane" title="Cell membrane">cell membrane</a>, or act as a <a href="/wiki/Nuclease" title="Nuclease">nuclease</a> to chop up the <a href="/wiki/DNA" title="DNA">DNA</a> or <a href="/wiki/RNA" title="RNA">RNA</a> of the target cell.<sup id="cite_ref-:0_5-1" class="reference"><a href="#cite_note-:0-5"><span class="cite-bracket">&#91;</span>5<span class="cite-bracket">&#93;</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Translocation">Translocation</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Colicin&amp;action=edit&amp;section=2" title="Edit section: Translocation"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Most colicins are able to translocate the outer membrane by a two-receptor system, where one receptor is used for the initial binding and the second for translocation. The initial binding is to <a href="/wiki/TonB-dependent_receptors" class="mw-redirect" title="TonB-dependent receptors">cell surface receptors</a> such as the outer membrane proteins OmpF, FepA, BtuB, Cir and FhuA; colicins have been classified according to which receptors they bind to. The presence of specific periplasmic proteins, such as <a href="/wiki/Outer_membrane_efflux_proteins" class="mw-redirect" title="Outer membrane efflux proteins">TolA, TolB, TolC</a>, or TonB, are required for translocation across the membrane.<sup id="cite_ref-PUB00014773_6-0" class="reference"><a href="#cite_note-PUB00014773-6"><span class="cite-bracket">&#91;</span>6<span class="cite-bracket">&#93;</span></a></sup> <a href="/wiki/Cloacin_immunity_protein" title="Cloacin immunity protein">Cloacin</a><sup id="cite_ref-pmid6253914_7-0" class="reference"><a href="#cite_note-pmid6253914-7"><span class="cite-bracket">&#91;</span>7<span class="cite-bracket">&#93;</span></a></sup> DF13 is a bacteriocin that inactivates ribosomes by hydrolysing 16S RNA in 30S ribosomes at a specific site.<sup id="cite_ref-PUB00006229_8-0" class="reference"><a href="#cite_note-PUB00006229-8"><span class="cite-bracket">&#91;</span>8<span class="cite-bracket">&#93;</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Resistance">Resistance</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Colicin&amp;action=edit&amp;section=3" title="Edit section: Resistance"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Because they target specific receptors and use specific translocation machinery, cells can make themselves resistant to the colicin by repressing or deleting the genes for these proteins. Such resistant cells may suffer the lack of a key nutrient (such as <a href="/wiki/Iron" title="Iron">iron</a> or a <a href="/wiki/Vitamin_B" class="mw-redirect" title="Vitamin B">B vitamin</a>), but benefit by not being killed. Colicins exhibit a '1-hit killing kinetic' <sup class="noprint Inline-Template Template-Fact" style="white-space:nowrap;">&#91;<i><a href="/wiki/Wikipedia:Citation_needed" title="Wikipedia:Citation needed"><span title="This claim needs references to reliable sources. (December 2018)">citation needed</span></a></i>&#93;</sup> which does not necessarily mean a single molecule is sufficient to kill, but certainly that it only takes a small number. In his 1969 Nobel Laureate speech, <a href="/wiki/Salvador_E._Luria" class="mw-redirect" title="Salvador E. Luria">Salvador E. Luria</a> speculated that colicins could only be this toxic by causing a <a href="/wiki/Domino_effect" title="Domino effect">domino effect</a> that destabilized the cell membrane.<sup id="cite_ref-9" class="reference"><a href="#cite_note-9"><span class="cite-bracket">&#91;</span>9<span class="cite-bracket">&#93;</span></a></sup> He was not entirely correct, but pore-forming colicins do depolarize the membrane and thus eliminate the energy source for the cell. The colicins are highly effective <a href="/wiki/Toxin" title="Toxin">toxins</a>.<sup class="noprint Inline-Template Template-Fact" style="white-space:nowrap;">&#91;<i><a href="/wiki/Wikipedia:Citation_needed" title="Wikipedia:Citation needed"><span title="This claim needs references to reliable sources. (December 2022)">citation needed</span></a></i>&#93;</sup> </p> <div class="mw-heading mw-heading2"><h2 id="Genetic_organisation">Genetic organisation</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Colicin&amp;action=edit&amp;section=4" title="Edit section: Genetic organisation"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Virtually all colicins are carried on <a href="/wiki/Plasmid" title="Plasmid">plasmids</a>. The two general classes of colicinogenic plasmids are large, low-copy-number plasmids, and small, high-copy-number plasmids. The larger plasmids carry other genes, as well as the colicin operon. The colicin operons are generally organized with several major <a href="/wiki/Gene" title="Gene">genes</a>. These include a colicin structural gene, an immunity gene, and a <a href="/w/index.php?title=Bacteriocin_release_protein&amp;action=edit&amp;redlink=1" class="new" title="Bacteriocin release protein (page does not exist)">bacteriocin release protein</a> (BRP), or <a href="/wiki/Lysis" title="Lysis">lysis</a>, gene. The immunity gene is often produced constitutively, while the BRP is generally produced only as a read-through of the <a href="/wiki/Stop_codon" title="Stop codon">stop codon</a> on the colicin structural gene. The colicin itself is repressed by the <a href="/wiki/SOS_response" title="SOS response">SOS response</a> and may be regulated in other ways as well.<sup id="cite_ref-10" class="reference"><a href="#cite_note-10"><span class="cite-bracket">&#91;</span>10<span class="cite-bracket">&#93;</span></a></sup> </p><p>Retaining the colicin plasmid is very important for cells that live with their relatives, because if a cell loses the immunity gene, it quickly becomes subject to destruction by circulating colicin. At the same time, colicin is only released from a producing cell by the use of the lysis protein, which results in that cell's death. This suicidal production mechanism would appear to be very costly, except for the fact that it is regulated by the <a href="/wiki/SOS_response" title="SOS response">SOS response</a>, which responds to significant <a href="/wiki/DNA" title="DNA">DNA</a> damage. In short, colicin production may only occur in terminally ill cells. The Professor Kleanthous Research Group at the <a href="/wiki/University_of_Oxford" title="University of Oxford">University of Oxford</a> study colicins extensively as a model system for characterising and investigating protein-protein interactions and recognition.<sup id="cite_ref-11" class="reference"><a href="#cite_note-11"><span class="cite-bracket">&#91;</span>11<span class="cite-bracket">&#93;</span></a></sup> </p><p>BACTIBASE<sup id="cite_ref-Hammami_2007_12-0" class="reference"><a href="#cite_note-Hammami_2007-12"><span class="cite-bracket">&#91;</span>12<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-Hammami_2010_13-0" class="reference"><a href="#cite_note-Hammami_2010-13"><span class="cite-bracket">&#91;</span>13<span class="cite-bracket">&#93;</span></a></sup> database is an open-access database for bacteriocins including colicins (<a rel="nofollow" class="external text" href="http://bactibase.hammamilab.org/bacteriocinslist.php?Name=colicin">view complete list</a>). </p> <div class="mw-heading mw-heading2"><h2 id="References">References</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Colicin&amp;action=edit&amp;section=5" title="Edit section: References"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <style data-mw-deduplicate="TemplateStyles:r1239543626">.mw-parser-output .reflist{margin-bottom:0.5em;list-style-type:decimal}@media screen{.mw-parser-output .reflist{font-size:90%}}.mw-parser-output .reflist .references{font-size:100%;margin-bottom:0;list-style-type:inherit}.mw-parser-output .reflist-columns-2{column-width:30em}.mw-parser-output .reflist-columns-3{column-width:25em}.mw-parser-output .reflist-columns{margin-top:0.3em}.mw-parser-output .reflist-columns ol{margin-top:0}.mw-parser-output .reflist-columns li{page-break-inside:avoid;break-inside:avoid-column}.mw-parser-output .reflist-upper-alpha{list-style-type:upper-alpha}.mw-parser-output .reflist-upper-roman{list-style-type:upper-roman}.mw-parser-output .reflist-lower-alpha{list-style-type:lower-alpha}.mw-parser-output .reflist-lower-greek{list-style-type:lower-greek}.mw-parser-output .reflist-lower-roman{list-style-type:lower-roman}</style><div class="reflist reflist-columns references-column-width reflist-columns-2"> <ol class="references"> <li id="cite_note-1"><span class="mw-cite-backlink"><b><a href="#cite_ref-1">^</a></b></span> <span class="reference-text"><style data-mw-deduplicate="TemplateStyles:r1238218222">.mw-parser-output cite.citation{font-style:inherit;word-wrap:break-word}.mw-parser-output .citation q{quotes:"\"""\"""'""'"}.mw-parser-output .citation:target{background-color:rgba(0,127,255,0.133)}.mw-parser-output .id-lock-free.id-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/6/65/Lock-green.svg")right 0.1em center/9px no-repeat}.mw-parser-output .id-lock-limited.id-lock-limited a,.mw-parser-output .id-lock-registration.id-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/d/d6/Lock-gray-alt-2.svg")right 0.1em center/9px no-repeat}.mw-parser-output .id-lock-subscription.id-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/a/aa/Lock-red-alt-2.svg")right 0.1em center/9px no-repeat}.mw-parser-output .cs1-ws-icon a{background:url("//upload.wikimedia.org/wikipedia/commons/4/4c/Wikisource-logo.svg")right 0.1em center/12px no-repeat}body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-free a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-limited a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-registration a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-subscription a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .cs1-ws-icon a{background-size:contain;padding:0 1em 0 0}.mw-parser-output .cs1-code{color:inherit;background:inherit;border:none;padding:inherit}.mw-parser-output .cs1-hidden-error{display:none;color:var(--color-error,#d33)}.mw-parser-output .cs1-visible-error{color:var(--color-error,#d33)}.mw-parser-output .cs1-maint{display:none;color:#085;margin-left:0.3em}.mw-parser-output .cs1-kern-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right{padding-right:0.2em}.mw-parser-output .citation .mw-selflink{font-weight:inherit}@media screen{.mw-parser-output .cs1-format{font-size:95%}html.skin-theme-clientpref-night .mw-parser-output .cs1-maint{color:#18911f}}@media screen and (prefers-color-scheme:dark){html.skin-theme-clientpref-os .mw-parser-output .cs1-maint{color:#18911f}}</style><cite id="CITEREFFeldgardenRiley1999" class="citation journal cs1">Feldgarden M, Riley MA (1999). "The phenotypic and fitness effects of colicin resistance in Escherichia coli K-12". <i>Evolution</i>. <b>53</b> (4): 1019–27. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.2307%2F2640807">10.2307/2640807</a>. <a href="/wiki/JSTOR_(identifier)" class="mw-redirect" title="JSTOR (identifier)">JSTOR</a>&#160;<a rel="nofollow" class="external text" href="https://www.jstor.org/stable/2640807">2640807</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&#160;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/28565527">28565527</a>.</cite><span title="ctx_ver=Z39.88-2004&amp;rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&amp;rft.genre=article&amp;rft.jtitle=Evolution&amp;rft.atitle=The+phenotypic+and+fitness+effects+of+colicin+resistance+in+Escherichia+coli+K-12&amp;rft.volume=53&amp;rft.issue=4&amp;rft.pages=1019-27&amp;rft.date=1999&amp;rft_id=info%3Apmid%2F28565527&amp;rft_id=https%3A%2F%2Fwww.jstor.org%2Fstable%2F2640807%23id-name%3DJSTOR&amp;rft_id=info%3Adoi%2F10.2307%2F2640807&amp;rft.aulast=Feldgarden&amp;rft.aufirst=M&amp;rft.au=Riley%2C+MA&amp;rfr_id=info%3Asid%2Fen.wikipedia.org%3AColicin" class="Z3988"></span></span> </li> <li id="cite_note-PUB00030669-2"><span class="mw-cite-backlink"><b><a href="#cite_ref-PUB00030669_2-0">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFKangPostleChenPark2004" class="citation journal cs1">Kang C, Postle K, Chen G, Park H, Youn B, Hilsenbeck JL (2004). <a rel="nofollow" class="external text" href="https://doi.org/10.1111%2Fj.1365-2958.2003.03884.x">"Crystal structure of the cytotoxic bacterial protein colicin B at 2.5 A resolution"</a>. <i>Mol. 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class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Colicin&amp;action=edit&amp;section=6" title="Edit section: External links"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <ul><li><a rel="nofollow" class="external text" href="https://web.archive.org/web/20070401085510/http://mbe.oxfordjournals.org/cgi/content/abstract/10/6/1380">Molecular mechanisms of colicin evolution</a> <a rel="nofollow" class="external text" href="https://web.archive.org/web/20060224032938/http://mbe.oxfordjournals.org/cgi/reprint/10/6/1380">pdf</a></li> <li><a rel="nofollow" class="external text" href="http://mic.sgmjournals.org/cgi/content/full/146/7/1671">The newly characterized colicin Y provides evidence of positive selection in pore-former colicin diversification</a></li> <li><a rel="nofollow" class="external text" href="http://opm.phar.umich.edu/families.php?superfamily=93">Colicin OPM database</a></li> <li><a rel="nofollow" class="external text" href="http://www.proteopedia.org/wiki/index.php/Colicin">3D interactive pages about colicins</a></li> <li><a rel="nofollow" class="external text" href="http://www.tcdb.org/tcdb/index.php?tc=1.C.1">Transport Classification Database listing for colicin</a></li> <li><a rel="nofollow" class="external text" href="http://www.ebi.ac.uk/pdbe-srv/view/search?search_type=advanced&amp;text=colicin">Protein Data Bank colicin listing</a></li></ul> <div role="note" style="font-style: italic;">This article incorporates text from the public domain <a href="/wiki/Pfam" title="Pfam">Pfam</a> and <a href="/wiki/InterPro" title="InterPro">InterPro</a>: <a rel="nofollow" class="external text" href="https://www.ebi.ac.uk/interpro/entry/IPR000290">IPR000290</a></div> <!-- NewPP limit report Parsed by mw‐web.eqiad.main‐5dc468848‐kwxnb Cached time: 20241122153337 Cache expiry: 2592000 Reduced expiry: false Complications: [vary‐revision‐sha1, show‐toc] CPU time usage: 0.293 seconds Real 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