1LLQ

Crystal Structure of Malic Enzyme from Ascaris suum Complexed with Nicotinamide Adenine Dinucleotide

1LLQ の概要

• エントリーDOI: 10.2210/pdb1llq/pdb
• 分子名称: NAD-dependent malic enzyme, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total)
• 機能のキーワード: rossmann fold, oxidoreductase
• 由来する生物種: Ascaris suum (pig roundworm)
• 細胞内の位置: Mitochondrion matrix: P27443
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 138439.66

構造登録者

Coleman, D.E.,Jagannatha, G.S.,Goldsmith, E.J.,Cook, P.F.,Harris, B.G. (登録日: 2002-04-29, 公開日: 2002-05-08, 最終更新日: 2023-08-16)

主引用文献

Coleman, D.E.,Rao, G.S.,Goldsmith, E.J.,Cook, P.F.,Harris, B.G.
Crystal structure of the malic enzyme from Ascaris suum complexed with nicotinamide adenine dinucleotide at 2.3 A resolution.
Biochemistry, 41:6928-6938, 2002

PubMed Abstract: The structure of the Ascaris suum mitochondrial NAD-malic enzyme in binary complex with NAD has been solved to a resolution of 2.3 A by X-ray crystallography. The structure resembles that of the human mitochondrial enzyme determined in complex with NAD [Xu, Y., Bhargava, G., Wu, H., Loeber, G., and Tong, L. (1999) Structure 7, 877-889]. The enzyme is a tetramer comprised of subunits possessing four domains organized in an "open" structure typical of the NAD-bound form. The subunit organization, as in the human enzyme, is a dimer of dimers. The Ascaris enzyme contains 30 additional residues at its amino terminus relative to the human enzyme. These residues significantly increase the interactions that promote tetramer formation and give rise to different subunit-subunit interactions. Unlike the mammalian enzyme, the Ascaris malic enzyme is not regulated by ATP, and no ATP binding site is observed in this structure. Although the active sites of the two enzymes are similar, residues interacting with NAD differ between the two. The structure is discussed in terms of the mechanism and particularly with respect to previously obtained kinetic and site-directed mutagenesis experiments.

PubMed: 12033925
DOI: 10.1021/bi0255120

実験手法

X-RAY DIFFRACTION (2.3 Å)