4qvb: Difference between revisions

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-'''Unreleased structure'''
+==Mycobacterium tuberculosis protein Rv1155 in complex with co-enzyme F420==
+<StructureSection load='4qvb' size='340' side='right' caption='[[4qvb]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4qvb]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QVB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QVB FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=F42:COENZYME+F420'>F42</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PDO:1,3-PROPANDIOL'>PDO</scene>, <scene name='pdbligand=PGO:S-1,2-PROPANEDIOL'>PGO</scene></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=4qvb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qvb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qvb RCSB], [http://www.ebi.ac.uk/pdbsum/4qvb PDBsum]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Coenzyme F420 is a deazaflavin hydride carrier with a lower reduction potential than most flavins. In Mycobacterium tuberculosis (Mtb), F420 plays an important role in activating PA-824, an anti-tuberculosis drug currently in clinical trials. Although F420 is important to Mtb redox metabolism, little is known about the enzymes that bind F420 and the reactions that they catalyze. We have identified a novel F420 -binding protein, Rv1155, which is annotated in the Mtb genome sequence as a putative flavin mononucleotide (FMN)-binding protein. Using biophysical techniques, we have demonstrated that instead of binding FMN or other flavins, Rv1155 binds coenzyme F420 . The crystal structure of the complex of Rv1155 and F420 reveals one F420 molecule bound to each monomer of the Rv1155 dimer. Structural, biophysical, and bioinformatic analyses of the Rv1155-F420 complex provide clues about its role in the bacterium. This article is protected by copyright. All rights reserved.
-The entry 4qvb is ON HOLD  until Paper Publication
+Molecular insights into the binding of coenzyme F to the conserved protein Rv1155 from Mycobacterium tuberculosis.,Mashalidis EH, Gittis AG, Tomczak A, Abell C, Barry CE 3rd, Garboczi DN Protein Sci. 2015 Jan 31. doi: 10.1002/pro.2645. PMID:25644473<ref>PMID:25644473</ref>
-Authors: Mashalidis, E.H., Gittis, A.G., Tomczak, A., Abell, C., Barry III, C.E., Garboczi, D.N.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description:
+== References ==
-[[Category: Unreleased Structures]]
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Abell, C]]
-[[Category: Garboczi, D.N]]
+[[Category: Garboczi, D N]]
-[[Category: Barry Iii, C.E]]
+[[Category: Gittis, A G]]
-[[Category: Gittis, A.G]]
+[[Category: III, C E.Barry]]
+[[Category: Mashalidis, E H]]
 [[Category: Tomczak, A]]
-[[Category: Mashalidis, E.H]]
+[[Category: Oxidoreductase]]