2pda: Difference between revisions

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[[Image:2pda.jpg|left|200px]]
{{Seed}}
[[Image:2pda.png|left|200px]]


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{{STRUCTURE_2pda|  PDB=2pda  |  SCENE=  }}  
{{STRUCTURE_2pda|  PDB=2pda  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN PYRUVATE-FERREDOXIN OXIDOREDUCTASE FROM DESULFOVIBRIO AFRICANUS AND PYRUVATE.'''
===CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN PYRUVATE-FERREDOXIN OXIDOREDUCTASE FROM DESULFOVIBRIO AFRICANUS AND PYRUVATE.===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_10048931}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 10048931 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10048931}}


==About this Structure==
==About this Structure==
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[[Category: Pyruvate catabolism]]
[[Category: Pyruvate catabolism]]
[[Category: Tpp-dependent enzyme]]
[[Category: Tpp-dependent enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 12:40:18 2008''
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