5ZI3

MDH3 wild type, apo-form

5ZI3 の概要

• エントリーDOI: 10.2210/pdb5zi3/pdb
• 分子名称: Malate dehydrogenase, GLYCEROL (3 entities in total)
• 機能のキーワード: malate dehydrogenase, glyoxysome, fatty acid oxidation, mdh3, oxidoreductase
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 74940.63

構造登録者

Moriyama, S.,Nishio, K.,Mizushima, T. (登録日: 2018-03-14, 公開日: 2018-10-24, 最終更新日: 2023-11-22)

主引用文献

Moriyama, S.,Nishio, K.,Mizushima, T.
Structure of glyoxysomal malate dehydrogenase (MDH3) from Saccharomyces cerevisiae.
Acta Crystallogr F Struct Biol Commun, 74:617-624, 2018

PubMed Abstract: Malate dehydrogenase (MDH), a carbohydrate and energy metabolism enzyme in eukaryotes, catalyzes the interconversion of malate to oxaloacetate (OAA) in conjunction with that of nicotinamide adenine dinucleotide (NAD) to NADH. Three isozymes of MDH have been reported in Saccharomyces cerevisiae: MDH1, MDH2 and MDH3. MDH1 is a mitochondrial enzyme and a member of the tricarboxylic acid cycle, whereas MDH2 is a cytosolic enzyme that functions in the glyoxylate cycle. MDH3 is a glyoxysomal enzyme that is involved in the reoxidation of NADH, which is produced during fatty-acid β-oxidation. The affinity of MDH3 for OAA is lower than those of MDH1 and MDH2. Here, the crystal structures of yeast apo MDH3, the MDH3-NAD complex and the MDH3-NAD-OAA ternary complex were determined. The structure of the ternary complex suggests that the active-site loop is in the open conformation, differing from the closed conformations in mitochondrial and cytosolic malate dehydrogenases.

PubMed: 30279312
DOI: 10.1107/S2053230X18011895

実験手法

X-RAY DIFFRACTION (2.1 Å)