Halophilic adaptation: Novel solvent protein interactions observed in the 2.9 and 2.6 Å Resolution structures of the wild type and a mutant of malate dehydrogenase from Haloarcula marismortui

Biochemistry

Volumn 39, Issue 5, 2000, Pages 992-1000

  Richard, Stéphane B ^a,c   Madern, Dominique ^a   Garcin, Elsa ^a,d   Zaccai, Giuseppe ^a,b,e  

^a CEA GRENOBLE   (France)

^b INSTITUT DE BIOLOGIE STRUCTURALE   (France)

^c SALK INSTITUTE FOR BIOLOGICAL STUDIES   (United States)

^d SCRIPPS RESEARCH INSTITUTE   (United States)

^e INSTITUT LAUE LANGEVIN   (France)

Author keywords

[No Author keywords available]

Indexed keywords

CHLORIDE ION; MALATE DEHYDROGENASE; SODIUM ION; SOLVENT; TETRAMER;

ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; HALOARCULA MARISMORTUI; HALOPHILIC BACTERIUM; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN STABILITY; SOLUBILITY;

ADAPTATION, PHYSIOLOGICAL; APOENZYMES; ARGININE; BINDING SITES; CATALYTIC DOMAIN; CATIONS, MONOVALENT; CHLORIDES; CRYSTALLOGRAPHY, X-RAY; GLUTAMIC ACID; HALOARCULA MARISMORTUI; HYDROGEN BONDING; MALATE DEHYDROGENASE; MUTAGENESIS, SITE-DIRECTED; SALTS; SODIUM; SOLVENTS; WATER;

ARCHAEA; BACTERIA (MICROORGANISMS); HALOARCULA MARISMORTUI; HARNESS;

EID: 0034620588     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi991001a     Document Type: Article

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