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The transcriptional regulator AfArsR responds to AsIII and SbIII by coordinating the metalloids with three cysteines, located in a short sequence of the same monomer chain. Here, we characterize the binding of AsIII and HgII to a model peptide encompassing this fragment of the protein via solution equilibrium and spectroscopic/spectrometric techniques (pH potentiometry, UV, CD, NMR, PAC, EXAFS, and ESI-MS) combined with DFT calculations and MD simulations. Coordination of AsIII changes the peptide structure from a random-coil to a well-defined structure of the complex. A trigonal pyramidal AsS3 binding site is formed with almost exactly the same structure as observed in the crystal structure of the native protein, implying that the peptide possesses all of the features required to mimic the AsIII recognition and response selectivity of AfArsR. Contrary to this, binding of HgII to the peptide does not lead to a well-defined structure of the peptide, and the atoms near the metal binding site are displaced and reoriented in the HgII model. Our model study suggests that structural organization of the metal site by the inducer ion is a key element in the mechanism of the metalloid-selective recognition of this protein. Tóth, Annamária; Sajdik, Kadosa; Gyurcsik, Béla; Nafaee, Zeyad H; Wéber, Edit; Kele, Zoltan; Christensen, Niels Johan; Schell, Juliana; Correia, Joao Guilherme; Clauss, Kajsa G V Sigfridsson; Pittkowski, Rebecca K; Thulstrup, Peter Waaben; Hemmingsen, Lars; Jancsó, Attila" /> <meta name="keywords" content="Ligands, Mercury, Metals, Monomers, Peptides and proteins" /> <script type="text/javascript" src="https://cds.cern.ch/js/jquery.min.js"></script>  <link rel="stylesheet" href="https://cds.cern.ch/img/webnews.css" type="text/css" />  <script type="text/javascript" src="https://cds.cern.ch/js/webnews.js?v=20131009"></script> <meta property="fb:app_id" content="137353533001720"/> <script type="text/x-mathjax-config"> MathJax.Hub.Config({ tex2jax: {inlineMath: [['$','$']], processEscapes: true}, showProcessingMessages: false, messageStyle: "none" }); </script> <script src="/MathJax/MathJax.js?config=TeX-AMS_CHTML" type="text/javascript"> </script>  <meta content="ACS : As$^{\textrm{III}}$ Selectively Induces a Disorder-to-Order Transition in the Metalloid Binding Region of the AfArsR Protein" name="citation_title" /> <meta content="Tóth, Annamária" name="citation_author" /> <meta content="Thulstrup, Peter Waaben" name="citation_author" /> <meta content="Jancsó, Attila" name="citation_author" /> <meta content="Gyurcsik, Béla" name="citation_author" /> <meta content="Wéber, Edit" name="citation_author" /> <meta content="Kele, Zoltan" name="citation_author" /> <meta content="Schell, Juliana" name="citation_author" /> <meta content="Christensen, Niels Johan" name="citation_author" /> <meta content="Clauss, Kajsa G V Sigfridsson" name="citation_author" /> <meta content="Nafaee, Zeyad H" name="citation_author" /> <meta content="Hemmingsen, Lars" name="citation_author" /> <meta content="Sajdik, Kadosa" name="citation_author" /> <meta content="Correia, Joao Guilherme" name="citation_author" /> <meta content="Pittkowski, Rebecca K" name="citation_author" /> <meta content="10.1021/jacs.3c11665" name="citation_doi" /> <meta content="J. 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The transcriptional regulator AfArsR responds to AsIII and SbIII by coordinating the metalloids with three cysteines, located in a short sequence of the same monomer chain. Here, we characterize the binding of AsIII and HgII to a model peptide encompassing this fragment of the protein via solution equilibrium and spectroscopic/spectrometric techniques (pH potentiometry, UV, CD, NMR, PAC, EXAFS, and ESI-MS) combined with DFT calculations and MD simulations. Coordination of AsIII changes the peptide structure from a random-coil to a well-defined structure of the complex. A trigonal pyramidal AsS3 binding site is formed with almost exactly the same structure as observed in the crystal structure of the native protein, implying that the peptide possesses all of the features required to mimic the AsIII recognition and response selectivity of AfArsR. Contrary to this, binding of HgII to the peptide does not lead to a well-defined structure of the peptide, and the atoms near the metal binding site are displaced and reoriented in the HgII model. Our model study suggests that structural organization of the metal site by the inducer ion is a key element in the mechanism of the metalloid-selective recognition of this protein." property="og:description" />  <meta content="summary" name="twitter:card" /> <style></style> </head> <body class="CERN32Document32Server search" lang="en">  <div id="cern-toolbar"> <h1><a href="http://cern.ch" title="CERN">CERN <span>Accelerating science</span></a></h1> <ul> <li class="cern-accountlinks"><a class="cern-account" href="https://cds.cern.ch/youraccount/login?ln=en&referer=https%3A//cds.cern.ch/record/2906013" title="Sign in to your CERN account">Sign in</a></li> <li><a class="cern-directory" href="http://cern.ch/directory" title="Search CERN resources and browse the directory">Directory</a></li> </ul> </div>   <div role="banner" class="clearfix" id="header"> <div class="header-inner inner"> <hgroup class="clearfix"> <h2 id="site-name"> <a rel="home" title="Home" href="/"><span>CERN Document Server</span></a> </h2> <h3 id="site-slogan">Access articles, reports and multimedia content in HEP</h3> </hgroup> <div role="navigation" id="main-navigation" class="cdsmenu"> <h2 class="element-invisible">Main menu</h2><ul class="links inline clearfix"> <li class="menu-386 first active-trail"><a class="active-trail" href="https://cds.cern.ch/?ln=en">Search</a></li> <li class="menu-444 "><a class="" title="" href="https://cds.cern.ch/submit?ln=en">Submit</a></li> <li class="menu-426 "><a class="" href="https://cds.cern.ch/help/?ln=en">Help</a></li> <li class="leaf hassubcdsmenu"> <a hreflang="en" class="header" href="https://cds.cern.ch/youraccount/display?ln=en">Personalize</a> <ul class="subsubcdsmenu"><li><a href="https://cds.cern.ch/youralerts/list?ln=en">Your alerts</a></li><li><a href="https://cds.cern.ch/yourbaskets/display?ln=en">Your baskets</a></li><li><a href="https://cds.cern.ch/yourcomments?ln=en">Your comments</a></li><li><a href="https://cds.cern.ch/youralerts/display?ln=en">Your searches</a></li></ul></li> </ul> </div> </div> </div>  <table class="navtrailbox"> <tr> <td class="navtrailboxbody"> <a href="/?ln=en" class="navtrail">Home</a> > As$^{\textrm{III}}$ Selectively Induces a Disorder-to-Order Transition in the Metalloid Binding Region of the AfArsR Protein </td> </tr> </table> </div> <div class="pagebody"><div class="pagebodystripemiddle"> <div class="detailedrecordbox"> <div class="detailedrecordtabs"> <div> <ul class="detailedrecordtabs"><li class="on first"><a href="/record/2906013/?ln=en">Information </a></li><li class=""><a href="/record/2906013/files?ln=en">Files </a></li></ul> <div id="tabsSpacer" style="clear:both;height:0px"> </div></div> </div> <div class="detailedrecordboxcontent"> <div class="top-left-folded"></div> <div class="top-right-folded"></div> <div class="inside">  <abbr class="unapi-id" title="2906013"></abbr> <style type="text/css">  </style> <table class="formatRecordTableFullWidth" > <tr> <td class="formatRecordHeader" style="background-image: url('https://cds.cern.ch/img/journals.jpg');" colspan="2">  Article </td> </tr> <script type="text/javascript"> $( document ).ready(function() { $('.showAuthor').on('click', function() { var author = '<p>' + $(this).data('name') + '</p>'; var affiliation = $(this).data('affiliation') + '</br>'; var contribution = $(this).data('contribution') + '</br>'; $.magnificPopup.open({ items: { src: '<div id="ovelary-mathjax" class="overlay-white oc-content overlay-white-500">' + author + affiliation + contribution + '</div>', type: 'inline' }, callbacks: { open: function() { var div = document.getElementById("overlay-mathjax") MathJax.Hub.Queue(["Typeset", MathJax.Hub, div]); }, } }) }) }); </script> <tr><td class="formatRecordLabel"> Title </td><td style="padding-left:5px;"><b>As$^{\textrm{III}}$ Selectively Induces a Disorder-to-Order Transition in the Metalloid Binding Region of the AfArsR Protein</b></td></tr> <tr><td class="formatRecordLabel"><span style="white-space:nowrap;"> Author(s) </span> </td><td style="padding-left:5px;"> <script type="text/javascript"> function toggle_authors_visibility(){ var more = document.getElementById('more'); var link = document.getElementById('link'); var extension = document.getElementById('extension'); if (more.style.display=='none'){ more.style.display = ''; extension.style.display = 'none'; link.innerHTML = "Hide" } else { more.style.display = 'none'; extension.style.display = ''; link.innerHTML = "Show all 14 authors" } link.style.color = "rgb(204,0,0);" } function set_up(){ var extension = document.getElementById('extension'); extension.innerHTML = ""; toggle_authors_visibility(); } </script> <a name="show_hide" /><a href="https://cds.cern.ch/search?f=author&p=T%C3%B3th%2C%20Annam%C3%A1ria&ln=en">Tóth, Annamária</a> ; <a href="https://cds.cern.ch/search?f=author&p=Sajdik%2C%20Kadosa&ln=en">Sajdik, Kadosa</a> ; <a href="https://cds.cern.ch/search?f=author&p=Gyurcsik%2C%20B%C3%A9la&ln=en">Gyurcsik, Béla</a> ; <a href="https://cds.cern.ch/search?f=author&p=Nafaee%2C%20Zeyad%20H&ln=en">Nafaee, Zeyad H</a> ; <a href="https://cds.cern.ch/search?f=author&p=W%C3%A9ber%2C%20Edit&ln=en">Wéber, Edit</a> ; <a href="https://cds.cern.ch/search?f=author&p=Kele%2C%20Zoltan&ln=en">Kele, Zoltan</a> ; <a href="https://cds.cern.ch/search?f=author&p=Christensen%2C%20Niels%20Johan&ln=en">Christensen, Niels Johan</a> ; <a href="https://cds.cern.ch/search?f=author&p=Schell%2C%20Juliana&ln=en">Schell, Juliana</a> (CERN) ; <a href="https://cds.cern.ch/search?f=author&p=Correia%2C%20Joao%20Guilherme&ln=en">Correia, Joao Guilherme</a> (CERN) ; <a href="https://cds.cern.ch/search?f=author&p=Clauss%2C%20Kajsa%20G%20V%20%20Sigfridsson&ln=en">Clauss, Kajsa G V Sigfridsson</a><span id="more" style=""> ; <a href="https://cds.cern.ch/search?f=author&p=Pittkowski%2C%20Rebecca%20K&ln=en">Pittkowski, Rebecca K</a> ; <a href="https://cds.cern.ch/search?f=author&p=Thulstrup%2C%20Peter%20Waaben&ln=en">Thulstrup, Peter Waaben</a> ; <a href="https://cds.cern.ch/search?f=author&p=Hemmingsen%2C%20Lars&ln=en">Hemmingsen, Lars</a> ; <a href="https://cds.cern.ch/search?f=author&p=Jancs%C3%B3%2C%20Attila&ln=en">Jancsó, Attila</a></span> <span id="extension"></span> <small><i><a id="link" href="#" onclick="toggle_authors_visibility()" style="color:rgb(204,0,0);"></a></i></small><script type="text/javascript">set_up()</script></td></tr> <tr><td class="formatRecordLabel"> Publication </td><td style="padding-left:5px;">2024</td></tr> <tr><td class="formatRecordLabel"> Number of pages </td><td style="padding-left:5px;">14</td></tr> <tr><td class="formatRecordLabel"> In: </td><td style="padding-left:5px;"><a href="http://dx.doi.org/10.1021/jacs.3c11665"><i>J. Am. Chem. Soc.</i> 146 (2024) 17009-17022</a> </a></td></tr> <tr><td class="formatRecordLabel"> DOI </td><td style="padding-left:5px;"><a href="http://dx.doi.org/10.1021/jacs.3c11665" title="DOI" target="_blank">10.1021/jacs.3c11665</a> <tr><td class="formatRecordLabel"> Abstract </td><td style="padding-left:5px;">Arsenic is highly toxic and a significant threat to human health, but certain bacteria have developed defense mechanisms initiated by AsIII binding to AsIII-sensing proteins of the ArsR family. The transcriptional regulator AfArsR responds to AsIII and SbIII by coordinating the metalloids with three cysteines, located in a short sequence of the same monomer chain. Here, we characterize the binding of AsIII and HgII to a model peptide encompassing this fragment of the protein via solution equilibrium and spectroscopic/spectrometric techniques (pH potentiometry, UV, CD, NMR, PAC, EXAFS, and ESI-MS) combined with DFT calculations and MD simulations. Coordination of AsIII changes the peptide structure from a random-coil to a well-defined structure of the complex. A trigonal pyramidal AsS3 binding site is formed with almost exactly the same structure as observed in the crystal structure of the native protein, implying that the peptide possesses all of the features required to mimic the AsIII recognition and response selectivity of AfArsR. Contrary to this, binding of HgII to the peptide does not lead to a well-defined structure of the peptide, and the atoms near the metal binding site are displaced and reoriented in the HgII model. Our model study suggests that structural organization of the metal site by the inducer ion is a key element in the mechanism of the metalloid-selective recognition of this protein.</td></tr> <tr><td class="formatRecordLabel"> Copyright/License </td><td style="padding-left:5px;">© 2024-2025 American Chemical Society (License: <a href="https://creativecommons.org/licenses/by/4.0/">CC-BY-4.0</a>)</td></tr> </table> <br/>Corresponding record in: <a href="http://inspirehep.net/record/2806322">Inspire</a> <small> </small> <br/> <br/><br/><div align="right"><div style="padding-bottom:2px;padding-top:30px;"><span class="moreinfo" style="margin-right:10px;"> <a href="" class="moreinfo">Back to search</a> </span></div></div> <div class="bottom-left-folded"><div class="recordlastmodifiedbox" style="position:relative;margin-left:1px"> Record created 2024-08-01, last modified 2024-08-13</div></div> <div class="bottom-right-folded" style="text-align:right;padding-bottom:2px;"> <span class="moreinfo" style="margin-right:10px;"><a href="/search?ln=en&p=recid%3A2906013&rm=wrd" class="moreinfo">Similar records</a></span></div> </div> </div> </div> <br/> <br /> <div class="detailedrecordminipanel"> <div class="top-left"></div><div class="top-right"></div> <div class="inside"> <div id="detailedrecordminipanelfile" style="width:33%;float:left;text-align:center;margin-top:0"> <div><small class="detailedRecordActions">Fulltext:</small> <br /><a href="/record/2906013/files/document.pdf"><img style="border:none" src="/img/file-icon-text-34x48.gif" alt="Download fulltext" /><br />PDF</a><br /></div> </div> <div id="detailedrecordminipanelreview" style="width:30%;float:left;text-align:center"> </div> <div id="detailedrecordminipanelactions" style="width:36%;float:right;text-align:right;"> <ul class="detailedrecordactions"> <li><a href="/yourbaskets/add?ln=en&recid=2906013">Add to personal basket</a></li> <li>Export as <a style="text-decoration:underline;font-weight:normal" href="/record/2906013/export/hx?ln=en">BibTeX</a>, <a style="text-decoration:underline;font-weight:normal" href="/record/2906013/export/hm?ln=en">MARC</a>, <a style="text-decoration:underline;font-weight:normal" href="/record/2906013/export/xm?ln=en">MARCXML</a>, <a style="text-decoration:underline;font-weight:normal" href="/record/2906013/export/xd?ln=en">DC</a>, <a style="text-decoration:underline;font-weight:normal" href="/record/2906013/export/xe?ln=en">EndNote</a>,  <a style="text-decoration:underline;font-weight:normal" href="/record/2906013/export/xn?ln=en">NLM</a>, <a style="text-decoration:underline;font-weight:normal" href="/record/2906013/export/xw?ln=en">RefWorks</a> </li> </ul> <div style='padding-left: 13px;'>  <div id="bookmark"></div> <div id="bookmark_sciencewise"></div> <style type="text/css"> #bookmark_sciencewise, #bookmark {float: left;} #bookmark_sciencewise li {padding: 2px; width: 25px;} #bookmark_sciencewise ul, #bookmark ul {list-style-image: none;} </style> <script type="text/javascript" src="/js/jquery.bookmark.min.js"></script> <style type="text/css">@import "/css/jquery.bookmark.css";</style> <script type="text/javascript">// <![CDATA[ $.bookmark.addSite('sciencewise', 'ScienceWise.info', 'https://cds.cern.ch/img/sciencewise.png', 'en', 'bookmark', 'http://sciencewise.info/bookmarks/cds:2906013/add'); $('#bookmark_sciencewise').bookmark({sites: ['sciencewise']}); $('#bookmark').bookmark({ sites: ['facebook', 'twitter', 'linkedin', 'google_plusone'], icons: '/img/bookmarks.png', url: 'https://cds.cern.ch/record/2906013', addEmail: true, title: "As$^{\\textrm{III}}$ Selectively Induces a Disorder-to-Order Transition in the Metalloid Binding Region of the AfArsR Protein", description: "Arsenic is highly toxic and a significant threat to human health, but certain bacteria have developed defense mechanisms initiated by AsIII binding to AsIII-sensing proteins of the ArsR family. The transcriptional regulator AfArsR responds to AsIII and SbIII by coordinating the metalloids with three cysteines, located in a short sequence of the same monomer chain. Here, we characterize the binding of AsIII and HgII to a model peptide encompassing this fragment of the protein via solution equilibrium and spectroscopic/spectrometric techniques (pH potentiometry, UV, CD, NMR, PAC, EXAFS, and ESI-MS) combined with DFT calculations and MD simulations. Coordination of AsIII changes the peptide structure from a random-coil to a well-defined structure of the complex. A trigonal pyramidal AsS3 binding site is formed with almost exactly the same structure as observed in the crystal structure of the native protein, implying that the peptide possesses all of the features required to mimic the AsIII recognition and response selectivity of AfArsR. Contrary to this, binding of HgII to the peptide does not lead to a well-defined structure of the peptide, and the atoms near the metal binding site are displaced and reoriented in the HgII model. Our model study suggests that structural organization of the metal site by the inducer ion is a key element in the mechanism of the metalloid-selective recognition of this protein." }); // ]]> </script>  </div> </div> <div style="clear:both;margin-bottom: 0;"></div> </div> <div class="bottom-left"></div><div class="bottom-right"></div> </div> </div></div> <footer id="footer" class="pagefooter clearfix">  <div class="pagefooterstripeleft"> CERN Document Server :: <a class="footer" href="https://cds.cern.ch/?ln=en">Search</a> :: <a class="footer" href="https://cds.cern.ch/submit?ln=en">Submit</a> :: <a class="footer" href="https://cds.cern.ch/youraccount/display?ln=en">Personalize</a> :: <a class="footer" href="https://cds.cern.ch/help/?ln=en">Help</a> :: <a class="footer" href="https://cern.service-now.com/service-portal?id=privacy_policy&se=CDS-Service" target="_blank">Privacy Notice</a> :: <a class="footer" href="https://repository.cern/content-policy" target="_blank">Content Policy</a> :: <a class="footer" href="https://repository.cern/terms" target="_blank">Terms and Conditions</a> <br /> Powered by <a class="footer" href="http://invenio-software.org/">Invenio</a> <br /> Maintained by <a class="footer" href="https://cern.service-now.com/service-portal?id=service_element&name=CDS-Service">CDS Service</a> - Need help? 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