4tvo
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==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 with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4TVO FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4tvo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tvo OCA], [https://pdbe.org/4tvo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tvo RCSB], [https://www.ebi.ac.uk/pdbsum/4tvo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tvo ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/MDH_MYCTU MDH_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> | |
| - | [[Category: | + | </div> |
| - | [[Category: Ferraris | + | <div class="pdbe-citations 4tvo" style="background-color:#fffaf0;"></div> |
| - | [[Category: Rizzi | + | |
| + | ==See Also== | ||
| + | *[[Malate Dehydrogenase 3D structures|Malate Dehydrogenase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mycobacterium tuberculosis H37Rv]] | ||
| + | [[Category: Ferraris DM]] | ||
| + | [[Category: Rizzi M]] | ||
Current revision
Structure of Malate Dehydrogenase from Mycobacterium tuberculosis
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