1NI4

HUMAN PYRUVATE DEHYDROGENASE

1NI4 の概要

• エントリーDOI: 10.2210/pdb1ni4/pdb
• 分子名称: Pyruvate dehydrogenase E1 component: Alpha subunit, Pyruvate dehydrogenase E1 component: Beta subunit, MAGNESIUM ION, ... (6 entities in total)
• 機能のキーワード: thiamin pyrophosphate, pyruvate, alpha-keto acid dehydrogenase, pyruvate dehydrogenase, oxidoreductase
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Mitochondrion matrix: P08559 P11177
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 159444.81

構造登録者

Ciszak, E.,Korotchkina, L.G.,Dominiak, P.M.,Sidhu, S.,Patel, M.S. (登録日: 2002-12-20, 公開日: 2003-06-17, 最終更新日: 2024-10-30)

主引用文献

Ciszak, E.M.,Korotchkina, L.G.,Dominiak, P.M.,Sidhu, S.,Patel, M.S.
Structural Basis for Flip-Flop Action of Thiamin Pyrophosphate-Dependent Enzymes Revealed by Human Pyruvate Dehydrogenase
J.Biol.Chem., 278:21240-21246, 2003

PubMed Abstract: The derivative of vitamin B1, thiamin pyrophosphate, is a cofactor of enzymes performing catalysis in pathways of energy production. In alpha2beta2-heterotetrameric human pyruvate dehydrogenase, this cofactor is used to cleave the Calpha-C(=O) bond of pyruvate followed by reductive acetyl transfer to lipoyl-dihydrolipoamide acetyltransferase. The dynamic nonequivalence of two, otherwise chemically equivalent, catalytic sites has not yet been understood. To understand the mechanism of action of this enzyme, we determined the crystal structure of the holo-form of human pyruvate dehydrogenase at 1.95-A resolution. We propose a model for the flip-flop action of this enzyme through a concerted approximately 2-A shuttle-like motion of its heterodimers. Similarity of thiamin pyrophosphate binding in human pyruvate dehydrogenase with functionally related enzymes suggests that this newly defined shuttle-like motion of domains is common to the family of thiamin pyrophosphate-dependent enzymes.

PubMed: 12651851
DOI: 10.1074/jbc.M300339200

実験手法

X-RAY DIFFRACTION (1.95 Å)