2PDA

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

2PDA の概要

• エントリーDOI: 10.2210/pdb2pda/pdb
• 分子名称: PROTEIN (PYRUVATE-FERREDOXIN OXIDOREDUCTASE), MAGNESIUM ION, CALCIUM ION, ... (7 entities in total)
• 機能のキーワード: oxidoreductase, pyruvate catabolism, iron-sulfur cluster, tpp-dependent enzyme, complex
• 由来する生物種: Desulfovibrio africanus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 270673.17

構造登録者

Chabriere, E.,Charon, M.H. (登録日: 1998-11-10, 公開日: 1999-04-23, 最終更新日: 2024-10-16)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3 Å)