1b0p
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(New page: 200px<br /><applet load="1b0p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b0p, resolution 2.31Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 21:26, 24 November 2007
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CRYSTAL STRUCTURE OF PYRUVATE-FERREDOXIN OXIDOREDUCTASE FROM DESULFOVIBRIO AFRICANUS
Overview
Oxidative decarboxylation of pyruvate to form acetyl-coenzyme A, a crucial, step in many metabolic pathways, is carried out in most aerobic organisms, by the multienzyme complex pyruvate dehydrogenase. In most anaerobes, the, same reaction is usually catalyzed by a single enzyme, pyruvate:ferredoxin, oxidoreductase (PFOR). Thus, PFOR is a potential target for drug design, against certain anaerobic pathogens. Here, we report the crystal, structures of the homodimeric Desulfovibrio africanus PFOR (data to 2.3 A, resolution), and of its complex with pyruvate (3.0 A resolution). The, structures show that each subunit consists of seven domains, one of which, affords protection against oxygen. The thiamin pyrophosphate (TPP), cofactor and the three [4Fe-4S] clusters are suitably arranged to provide, a plausible electron transfer pathway. In addition, the PFOR-pyruvate, complex structure shows the noncovalent fixation of the substrate before, the catalytic reaction.
About this Structure
1B0P is a Single protein structure of sequence from Desulfovibrio africanus with MG, CA, SF4 and TPP as ligands. Active as Pyruvate synthase, with EC number 1.2.7.1 Full crystallographic information is available from OCA.
Reference
Crystal structures of the key anaerobic enzyme pyruvate:ferredoxin oxidoreductase, free and in complex with pyruvate., Chabriere E, Charon MH, Volbeda A, Pieulle L, Hatchikian EC, Fontecilla-Camps JC, Nat Struct Biol. 1999 Feb;6(2):182-90. PMID:10048931
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