Binding Studies and Structure Determination of the Recombinantly Produced Type-II 3-Dehydroquinate Dehydratase from Acinetobacter Baumannii

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Determination of the Recombinantly Produced Type-II 3-Dehydroquinate Dehydratase from Acinetobacter Baumannii </title> <meta name="description" content="Binding Studies and Structure Determination of the Recombinantly Produced Type-II 3-Dehydroquinate Dehydratase from Acinetobacter Baumannii "> <meta name="keywords" content="acinetobacter Bauman Nii, dehydroquinate dehydratase, dodecamer, open conformation"> <meta name="viewport" content="width=device-width, initial-scale=1, minimum-scale=1, maximum-scale=1, user-scalable=no"> <meta charset="utf-8"> <link href="https://cdn.waset.org/favicon.ico" type="image/x-icon" rel="shortcut icon"> <link href="https://cdn.waset.org/static/plugins/bootstrap-4.2.1/css/bootstrap.min.css" rel="stylesheet"> <link href="https://cdn.waset.org/static/plugins/fontawesome/css/all.min.css" rel="stylesheet"> <link href="https://cdn.waset.org/static/css/site.css?v=150220211555" rel="stylesheet"> </head> <body> <header> <div class="container"> <nav class="navbar 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class="card-body"><strong>Paper Count:</strong> 87351</div> </div> </div> </div> <div class="card publication-listing mt-3 mb-3"> <h5 class="card-header" style="font-size:.9rem">Binding Studies and Structure Determination of the Recombinantly Produced Type-II 3-Dehydroquinate Dehydratase from Acinetobacter Baumannii </h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Naseer%20Iqbal">Naseer Iqbal</a>, <a href="https://publications.waset.org/abstracts/search?q=Mukesh%20Kumar"> Mukesh Kumar</a>, <a href="https://publications.waset.org/abstracts/search?q=Pradeep%20Sharma"> Pradeep Sharma</a>, <a href="https://publications.waset.org/abstracts/search?q=Satya%20Prakash%20Yadav"> Satya Prakash Yadav</a>, <a href="https://publications.waset.org/abstracts/search?q=Punit%20Kaur"> Punit Kaur</a>, <a href="https://publications.waset.org/abstracts/search?q=Sujata%20%20Sharma"> Sujata Sharma</a>, <a href="https://publications.waset.org/abstracts/search?q=T.%20P.%20Singh"> T. P. Singh</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Dehydroquinase (3-dehydroquinate dehydratase, DHQD, EC 4.2.1.10) is involved in shikimate pathway and catalyzes the conversion of dehydroquinate to dehydroshikimate. Shikimate pathway is important drug target as this pathway is absent in mammals. DHQD from Acinetobacter baumannii (AbDHQD) was cloned, expressed and purified to homogeneity. The binding studies showed that compounds quinic acid and citrazinic acid bound to AbDHQD at micromolar concentrations. AbDHQD was crystallized using 30% PEG-3350, 50mM tris-HCl, and 1.0M MgSO4 at PH 8.0. Crystals of AbDHQD were stabilized by transferring them into reservoir solution to which 25% glycerol was added for data collection at 100K. The X-ray intensity data were collected to 2.0Å resolution. The crystals belong to monoclinic space group P21 with cell dimensions, a = 82.3, b = 95.3, c = 132.3Å and β = 95.7°. The structure was solved with molecular replacement method and refined to Rcryst/Rfree factors of 0.200/0.232. The structures of 12 crystallographically independent molecules in the asymmetry unit were identical with r.m.s shifts for the C atoms ranging from 0.3 Å to 0.8 Å. They formed a dodecamer with four trimers arranged in a tetrahedral manner. The classical lid adopted an open conformation although a sulfate ion was observed in the substrate binding site. As a result of which, the compounds quinic acid and citrazinic acid did not bind to AbDHQD. <iframe src="https://publications.waset.org/abstracts/60811.pdf" style="width:100%; height:400px;" frameborder="0"></iframe> <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=acinetobacter%20Bauman%20Nii" title="acinetobacter Bauman Nii">acinetobacter Bauman Nii</a>, <a href="https://publications.waset.org/abstracts/search?q=dehydroquinate%20dehydratase" title=" dehydroquinate dehydratase"> dehydroquinate dehydratase</a>, <a href="https://publications.waset.org/abstracts/search?q=dodecamer" title=" dodecamer"> dodecamer</a>, <a href="https://publications.waset.org/abstracts/search?q=open%20conformation" title=" open conformation"> open conformation</a> </p> <a href="https://publications.waset.org/abstracts/60811/binding-studies-and-structure-determination-of-the-recombinantly-produced-type-ii-3-dehydroquinate-dehydratase-from-acinetobacter-baumannii" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/60811.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">361</span> </span> </div> </div> </div> </main> <footer> <div id="infolinks" class="pt-3 pb-2"> <div class="container"> <div style="background-color:#f5f5f5;" class="p-3"> <div class="row"> <div class="col-md-2"> <ul class="list-unstyled"> About <li><a href="https://waset.org/page/support">About Us</a></li> <li><a href="https://waset.org/page/support#legal-information">Legal</a></li> <li><a target="_blank" rel="nofollow" href="https://publications.waset.org/static/files/WASET-16th-foundational-anniversary.pdf">WASET celebrates its 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Binding Studies and Structure Determination of the Recombinantly Produced Type-II 3-Dehydroquinate Dehydratase from Acinetobacter Baumannii