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3tqb

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Structure of the dihydrofolate reductase (folA) from Coxiella burnetii in complex with folate

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 ==Structure of the dihydrofolate reductase (folA) from Coxiella burnetii in complex with folate==
-<StructureSection load='3tqb' size='340' side='right' caption='[[3tqb]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+<StructureSection load='3tqb' size='340' side='right'caption='[[3tqb]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3tqb]] 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=3TQB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TQB FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3tqb]] 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=3TQB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TQB FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FOL:FOLIC+ACID'>FOL</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3tq8|3tq8]], [[3tq9|3tq9]], [[3tqa|3tqa]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FOL:FOLIC+ACID'>FOL</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CBU_1993, folA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=777 "Rickettsia burneti" (sic) Derrick 1939])</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=3tqb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tqb OCA], [https://pdbe.org/3tqb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tqb RCSB], [https://www.ebi.ac.uk/pdbsum/3tqb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tqb ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrofolate_reductase Dihydrofolate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.3 1.5.1.3] </span></td></tr>
-<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=3tqb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tqb OCA], [http://pdbe.org/3tqb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3tqb RCSB], [http://www.ebi.ac.uk/pdbsum/3tqb PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/Q83AB2_COXBU Q83AB2_COXBU]] Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.[PIRNR:PIRNR000194]
+[https://www.uniprot.org/uniprot/Q83AB2_COXBU Q83AB2_COXBU] Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.[PIRNR:PIRNR000194]
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-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.
-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>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3tqb" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Dihydrofolate reductase|Dihydrofolate reductase]]
+*[[Dihydrofolate reductase 3D structures|Dihydrofolate reductase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Dihydrofolate reductase]]
+[[Category: Coxiella burnetii]]
-[[Category: Cassidy, M]]
+[[Category: Large Structures]]
-[[Category: Franklin, M C]]
+[[Category: Cassidy M]]
-[[Category: Hillerich, B]]
+[[Category: Franklin MC]]
-[[Category: Love, J]]
+[[Category: Hillerich B]]
-[[Category: Oxidoreductase-oxidoreductase inhibitor complex]]
+[[Category: Love J]]

3tqb

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Structure of the dihydrofolate reductase (folA) from Coxiella burnetii in complex with folate

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