1EFL

HUMAN MALIC ENZYME IN A QUATERNARY COMPLEX WITH NAD, MG, AND TARTRONATE

1EFL の概要

• エントリーDOI: 10.2210/pdb1efl/pdb
• 関連するPDBエントリー: 1DO8 1EFK 1QR6
• 分子名称: MALIC ENZYME, MAGNESIUM ION, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (5 entities in total)
• 機能のキーワード: closed form, malic enzyme, complex, tartronate, oxidoreductase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Mitochondrion matrix: P23368
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 270776.30

構造登録者

Yang, Z.,Floyd, D.L.,Loeber, G.,Tong, L. (登録日: 2000-02-09, 公開日: 2000-03-08, 最終更新日: 2024-10-30)

主引用文献

Yang, Z.,Floyd, D.L.,Loeber, G.,Tong, L.
Structure of a closed form of human malic enzyme and implications for catalytic mechanism.
Nat.Struct.Biol., 7:251-257, 2000

PubMed Abstract: Malic enzymes are widely distributed in nature and have many biological functions. The crystal structure of human mitochondrial NAD(P)+-dependent malic enzyme in a quaternary complex with NAD+, Mn++ and oxalate has been determined at 2.2 A resolution. The structures of the quaternary complex with NAD+, Mg++, tartronate or ketomalonate have been determined at 2.6 A resolution. The structures show the enzyme in a closed form in these complexes and reveal the binding modes of the cation and the inhibitors. The divalent cation is coordinated in an octahedral fashion by six ligating oxygens, two from the substrate/inhibitor, three from Glu 255, Asp 256 and Asp 279 of the enzyme, and one from a water molecule. The structural information has significant implications for the catalytic mechanism of malic enzymes and identifies Tyr 112 and Lys 183 as possible catalytic residues. Changes in tetramer organization of the enzyme are also observed in these complexes, which might be relevant for its cooperative behavior and allosteric control.

PubMed: 10700286
DOI: 10.1038/73378

実験手法

X-RAY DIFFRACTION (2.6 Å)