3tr0: Difference between revisions
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==Structure of guanylate kinase (gmk) from Coxiella burnetii== | ==Structure of guanylate kinase (gmk) from Coxiella burnetii== | ||
<StructureSection load='3tr0' size='340' side='right' caption='[[3tr0]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='3tr0' size='340' side='right'caption='[[3tr0]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3tr0]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3tr0]] 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=3TR0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TR0 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.851Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5GP:GUANOSINE-5-MONOPHOSPHATE'>5GP</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3tr0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tr0 OCA], [https://pdbe.org/3tr0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tr0 RCSB], [https://www.ebi.ac.uk/pdbsum/3tr0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tr0 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/KGUA_COXBU KGUA_COXBU] Essential for recycling GMP and indirectly, cGMP.[HAMAP-Rule:MF_00328] | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 22: | Line 21: | ||
==See Also== | ==See Also== | ||
*[[Guanylate kinase|Guanylate kinase]] | *[[Guanylate kinase 3D structures|Guanylate kinase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Coxiella burnetii]] | ||
[[Category: Burshteyn | [[Category: Large Structures]] | ||
[[Category: Cassidy | [[Category: Burshteyn F]] | ||
[[Category: Cheung | [[Category: Cassidy M]] | ||
[[Category: Franklin | [[Category: Cheung J]] | ||
[[Category: Gary | [[Category: Franklin M]] | ||
[[Category: Love | [[Category: Gary E]] | ||
[[Category: Rudolph | [[Category: Love J]] | ||
[[Category: Rudolph M]] | |||
Latest revision as of 09:49, 27 November 2024
Structure of guanylate kinase (gmk) from Coxiella burnetiiStructure of guanylate kinase (gmk) from Coxiella burnetii
Structural highlights
FunctionKGUA_COXBU Essential for recycling GMP and indirectly, cGMP.[HAMAP-Rule:MF_00328] Publication Abstract from PubMedCoxiella 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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