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Crystal structures of the key anaerobic enzyme pyruvate:ferredoxin oxidoreductase, free and in complex with pyruvate
- Source :
- Nature Structural and Molecular Biology; February 1999, Vol. 6 Issue: 2 p182-190, 9p
- Publication Year :
- 1999
-
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 Å resolution), and of its complex with pyruvate (3.0 Å 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.
Details
- Language :
- English
- ISSN :
- 15459993 and 15459985
- Volume :
- 6
- Issue :
- 2
- Database :
- Supplemental Index
- Journal :
- Nature Structural and Molecular Biology
- Publication Type :
- Periodical
- Accession number :
- ejs25307049
- Full Text :
- https://doi.org/10.1038/5870