3mve
From Proteopedia
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| - | + | ==Crystal structure of a novel pyruvate decarboxylase== | |
| - | === | + | <StructureSection load='3mve' size='340' side='right' caption='[[3mve]], [[Resolution|resolution]] 2.20Å' scene=''> |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[3mve]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_27562 Atcc 27562]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MVE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MVE 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=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">frsA, VV1_0328 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=672 ATCC 27562])</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=3mve FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mve OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mve RCSB], [http://www.ebi.ac.uk/pdbsum/3mve PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The interaction between fermentation-respiration switch (FrsA) protein and glucose-specific enzyme IIA(Glc) increases glucose fermentation under oxygen-limited conditions. We show that FrsA converts pyruvate to acetaldehyde and carbon dioxide in a cofactor-independent manner and that its pyruvate decarboxylation activity is enhanced by the dephosphorylated form of IIA(Glc) (d-IIA(Glc)). Crystal structures of FrsA and its complex with d-IIA(Glc) revealed residues required for catalysis as well as the structural basis for the activation by d-IIA(Glc). | ||
| - | + | FrsA functions as a cofactor-independent decarboxylase to control metabolic flux.,Lee KJ, Jeong CS, An YJ, Lee HJ, Park SJ, Seok YJ, Kim P, Lee JH, Lee KH, Cha SS Nat Chem Biol. 2011 May 29. PMID:21623357<ref>PMID:21623357</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| - | [[Category: | + | == References == |
| - | [[Category: An, Y J | + | <references/> |
| - | [[Category: Cha, S S | + | __TOC__ |
| - | [[Category: Jeong, C S | + | </StructureSection> |
| + | [[Category: Atcc 27562]] | ||
| + | [[Category: An, Y J]] | ||
| + | [[Category: Cha, S S]] | ||
| + | [[Category: Jeong, C S]] | ||
[[Category: Fermentation/respiration switch protein]] | [[Category: Fermentation/respiration switch protein]] | ||
[[Category: Frsa]] | [[Category: Frsa]] | ||
[[Category: Hydrolase activator]] | [[Category: Hydrolase activator]] | ||
[[Category: Lyase]] | [[Category: Lyase]] | ||
Revision as of 09:45, 17 December 2014
Crystal structure of a novel pyruvate decarboxylase
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