3tqi

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Current revision (10:10, 1 March 2024) (edit) (undo)
 
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<StructureSection load='3tqi' size='340' side='right'caption='[[3tqi]], [[Resolution|resolution]] 2.84&Aring;' scene=''>
<StructureSection load='3tqi' size='340' side='right'caption='[[3tqi]], [[Resolution|resolution]] 2.84&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3tqi]] is a 4 chain structure with sequence from [https://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=3TQI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TQI FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3tqi]] is a 4 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=3TQI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TQI FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CBU_1341, guaA ([https://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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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.84&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/GMP_synthase_(glutamine-hydrolyzing) GMP synthase (glutamine-hydrolyzing)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.5.2 6.3.5.2] </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=3tqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tqi OCA], [https://pdbe.org/3tqi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tqi RCSB], [https://www.ebi.ac.uk/pdbsum/3tqi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tqi ProSAT]</span></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=3tqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tqi OCA], [https://pdbe.org/3tqi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tqi RCSB], [https://www.ebi.ac.uk/pdbsum/3tqi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tqi ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/GUAA_COXBU GUAA_COXBU]] Catalyzes the synthesis of GMP from XMP.[HAMAP-Rule:MF_00344]
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[https://www.uniprot.org/uniprot/GUAA_COXBU GUAA_COXBU] Catalyzes the synthesis of GMP from XMP.[HAMAP-Rule:MF_00344]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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<div class="pdbe-citations 3tqi" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[GMP synthase|GMP synthase]]
*[[GMP synthase|GMP synthase]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Coxiella burnetii]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Burshteyn, F]]
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[[Category: Burshteyn F]]
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[[Category: Cassidy, M]]
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[[Category: Cassidy M]]
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[[Category: Cheung, J]]
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[[Category: Cheung J]]
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[[Category: Franklin, M C]]
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[[Category: Franklin MC]]
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[[Category: Gary, E]]
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[[Category: Gary E]]
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[[Category: Love, J]]
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[[Category: Love J]]
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[[Category: Rudolph, M]]
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[[Category: Rudolph M]]
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[[Category: Gmp synthase]]
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[[Category: Ligase]]
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Current revision

Structure of the GMP synthase (guaA) from Coxiella burnetii

PDB ID 3tqi

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