1A5Z

LACTATE DEHYDROGENASE FROM THERMOTOGA MARITIMA (TMLDH)

Summary for 1A5Z

• Entry DOI: 10.2210/pdb1a5z/pdb
• Descriptor: L-LACTATE DEHYDROGENASE, 1,6-di-O-phosphono-beta-D-fructofuranose, CADMIUM ION, ... (6 entities in total)
• Functional Keywords: oxidoreductase, glycolysis, hyperthermophiles, thermotoga maritima, protein stability
• Biological source: Thermotoga maritima
• Cellular location: Cytoplasm: P16115
• Total number of polymer chains: 1
• Total formula weight: 36796.33

Authors

Auerbach, G.,Ostendorp, R.,Prade, L.,Korndoerfer, I.,Dams, T.,Huber, R.,Jaenicke, R. (deposition date: 1998-02-18, release date: 1999-03-23, Last modification date: 2024-10-23)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.1 Å)