4tvo
From Proteopedia
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| - | ''' | + | ==Structure of Malate Dehydrogenase from Mycobacterium tuberculosis== |
| + | <StructureSection load='4tvo' size='340' side='right' caption='[[4tvo]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4tvo]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TVO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TVO FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Malate_dehydrogenase Malate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.37 1.1.1.37] </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=4tvo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tvo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4tvo RCSB], [http://www.ebi.ac.uk/pdbsum/4tvo PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/I6XB21_MYCTU I6XB21_MYCTU]] Catalyzes the reversible oxidation of malate to oxaloacetate.[HAMAP-Rule:MF_01517] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The tricarboxylic acid (TCA) cycle is a central metabolic pathway of all aerobic organisms and is responsible for the synthesis of many important precursors and molecules. TCA cycle plays a key role in the metabolism of M. tuberculosis and is involved in the adaptation process of the bacteria to the host immune response. We present here the first crystal structures of M. tuberculosis malate dehydrogenase and citrate synthase, two consecutive enzymes of the tricarboxylic acid cycle, at 2.6 A and 1.5 A resolution, respectively. General analogies and local differences with the previously reported homologous protein structures are described. This article is protected by copyright. All rights reserved. | ||
| - | + | Structures of citrate synthase and malate dehydrogenase of mycobacterium tuberculosis.,Ferraris DM, Spallek R, Oehlmann W, Singh M, Rizzi M Proteins. 2014 Dec 18. doi: 10.1002/prot.24743. PMID:25524525<ref>PMID:25524525</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| - | [[Category: Ferraris, D | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Malate dehydrogenase]] | ||
| + | [[Category: Ferraris, D M]] | ||
[[Category: Rizzi, M]] | [[Category: Rizzi, M]] | ||
| + | [[Category: Krebs cycle]] | ||
| + | [[Category: Oxidoreductase]] | ||
Revision as of 13:34, 14 January 2015
Structure of Malate Dehydrogenase from Mycobacterium tuberculosis
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