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3trd

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==Structure of an alpha-beta serine hydrolase homologue from Coxiella burnetii==
==Structure of an alpha-beta serine hydrolase homologue from Coxiella burnetii==
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<StructureSection load='3trd' size='340' side='right' caption='[[3trd]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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<StructureSection load='3trd' size='340' side='right'caption='[[3trd]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3trd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"rickettsia_burneti"_(sic)_derrick_1939 "rickettsia burneti" (sic) derrick 1939]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TRD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TRD FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3trd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Coxiella_burnetii Coxiella burnetii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TRD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TRD FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CBU_1769 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=777 "Rickettsia burneti" (sic) Derrick 1939])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3trd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3trd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3trd RCSB], [http://www.ebi.ac.uk/pdbsum/3trd PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3trd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3trd OCA], [https://pdbe.org/3trd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3trd RCSB], [https://www.ebi.ac.uk/pdbsum/3trd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3trd ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q83AV9_COXBU Q83AV9_COXBU]
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Coxiella burnetii is a highly infectious bacterium and potential agent of bioterrorism. However, it has not been studied as extensively as other biological agents, and very few of its proteins have been structurally characterized. To address this situation, we undertook a study of critical metabolic enzymes in C. burnetii that have great potential as drug targets. We used high-throughput techniques to produce novel crystal structures of 48 of these proteins. We selected one protein, C. burnetii dihydrofolate reductase (CbDHFR), for additional work to demonstrate the value of these structures for structure-based drug design. This enzyme's structure reveals a feature in the substrate binding groove that is different between CbDHFR and human dihydrofolate reductase (hDFHR). We then identified a compound by in silico screening that exploits this binding groove difference, and demonstrated that this compound inhibits CbDHFR with at least 25-fold greater potency than hDHFR. Since this binding groove feature is shared by many other prokaryotes, the compound identified could form the basis of a novel antibacterial agent effective against a broad spectrum of pathogenic bacteria. This article is protected by copyright. All rights reserved.
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Structural Genomics for Drug Design against the Pathogen Coxiella burnetii.,Franklin MC, Cheung J, Rudolph MJ, Burshteyn F, Cassidy M, Gary E, Hillerich B, Yao ZK, Carlier PR, Totrov M, Love JD Proteins. 2015 Jun 1. doi: 10.1002/prot.24841. PMID:26033498<ref>PMID:26033498</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Burshteyn, F]]
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[[Category: Coxiella burnetii]]
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[[Category: Cassidy, M]]
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[[Category: Large Structures]]
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[[Category: Cheung, J]]
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[[Category: Burshteyn F]]
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[[Category: Franklin, M C]]
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[[Category: Cassidy M]]
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[[Category: Gary, E]]
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[[Category: Cheung J]]
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[[Category: Love, J]]
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[[Category: Franklin MC]]
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[[Category: Rudolph, M]]
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[[Category: Gary E]]
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[[Category: Cellular process]]
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[[Category: Love J]]
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[[Category: Hydrolase]]
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[[Category: Rudolph M]]

Current revision

Structure of an alpha-beta serine hydrolase homologue from Coxiella burnetii

PDB ID 3trd

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