This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

3tqj

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Structure of the superoxide dismutase (Fe) (sodB) from Coxiella burnetii

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3tqj"

@@ Line 3: / Line 3: @@
 <StructureSection load='3tqj' size='340' side='right'caption='[[3tqj]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3tqj]] is a 2 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=3TQJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TQJ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3tqj]] is a 2 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=3TQJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TQJ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</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]] 2.004&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CBU_1708, sodB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=777 "Rickettsia burneti" (sic) Derrick 1939])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] </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=3tqj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tqj OCA], [https://pdbe.org/3tqj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tqj RCSB], [https://www.ebi.ac.uk/pdbsum/3tqj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tqj ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/SODF_COXBU SODF_COXBU]] Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
+[https://www.uniprot.org/uniprot/SODF_COXBU SODF_COXBU] Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
-<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 3tqj" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
+[[Category: Coxiella burnetii]]
 [[Category: Large Structures]]
-[[Category: Superoxide dismutase]]
+[[Category: Cassidy M]]
-[[Category: Cassidy, M]]
+[[Category: Cheung J]]
-[[Category: Cheung, J]]
+[[Category: Franklin MC]]
-[[Category: Franklin, M C]]
+[[Category: Love J]]
-[[Category: Love, J]]
-[[Category: Oxidoreductase]]

3tqj

From Proteopedia

Current revision

Structure of the superoxide dismutase (Fe) (sodB) from Coxiella burnetii

Structural highlights

Function

See Also

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox