1B0P

CRYSTAL STRUCTURE OF PYRUVATE-FERREDOXIN OXIDOREDUCTASE FROM DESULFOVIBRIO AFRICANUS

Summary for 1B0P

• Entry DOI: 10.2210/pdb1b0p/pdb
• Descriptor: PROTEIN (PYRUVATE-FERREDOXIN OXIDOREDUCTASE), MAGNESIUM ION, CALCIUM ION, ... (6 entities in total)
• Functional Keywords: oxidoreductase, pyruvate catabolism, iron-sulfur cluster, tpp-dependent enzyme
• Biological source: Desulfovibrio africanus
• Cellular location: Cytoplasm : P94692
• Total number of polymer chains: 2
• Total formula weight: 270497.05

Authors

Chabriere, E.,Charon, M.H.,Volbeda, A. (deposition date: 1998-11-12, release date: 1999-04-23, Last modification date: 2023-12-27)

Primary citation

Chabriere, E.,Charon, M.H.,Volbeda, A.,Pieulle, L.,Hatchikian, E.C.,Fontecilla-Camps, J.C.
Crystal structures of the key anaerobic enzyme pyruvate:ferredoxin oxidoreductase, free and in complex with pyruvate.
Nat.Struct.Biol., 6:182-190, 1999

PubMed Abstract: 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.

PubMed: 10048931
DOI: 10.1038/5870

Experimental method

X-RAY DIFFRACTION (2.31 Å)