1A5Z

LACTATE DEHYDROGENASE FROM THERMOTOGA MARITIMA (TMLDH)

1A5Z の概要

• エントリーDOI: 10.2210/pdb1a5z/pdb
• 分子名称: L-LACTATE DEHYDROGENASE, 1,6-di-O-phosphono-beta-D-fructofuranose, CADMIUM ION, ... (6 entities in total)
• 機能のキーワード: oxidoreductase, glycolysis, hyperthermophiles, thermotoga maritima, protein stability
• 由来する生物種: Thermotoga maritima
• 細胞内の位置: Cytoplasm: P16115
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36796.33

構造登録者

Auerbach, G.,Ostendorp, R.,Prade, L.,Korndoerfer, I.,Dams, T.,Huber, R.,Jaenicke, R. (登録日: 1998-02-18, 公開日: 1999-03-23, 最終更新日: 2024-10-23)

主引用文献

Auerbach, G.,Ostendorp, R.,Prade, L.,Korndorfer, I.,Dams, T.,Huber, R.,Jaenicke, R.
Lactate dehydrogenase from the hyperthermophilic bacterium thermotoga maritima: the crystal structure at 2.1 A resolution reveals strategies for intrinsic protein stabilization.
Structure, 6:769-781, 1998

PubMed Abstract: L(+)-Lactate dehydrogenase (LDH) catalyzes the last step in anaerobic glycolysis, the conversion of pyruvate to lactate, with the concomitant oxidation of NADH. Extensive physicochemical and structural investigations of LDHs from both mesophilic and thermophilic organisms have been undertaken in order to study the temperature adaptation of proteins. In this study we aimed to determine the high-resolution structure of LDH from the hyperthermophilic bacterium Thermotoga maritima (TmLDH), the most thermostable LDH to be isolated so far. It was hoped that the structure of TmLDH would serve as a model system to reveal strategies of protein stabilization at temperatures near the boiling point of water.

PubMed: 9655830
DOI: 10.1016/S0969-2126(98)00078-1

実験手法

X-RAY DIFFRACTION (2.1 Å)