The 2.9 Å resolution crystal structure of malate dehydrogenase from Archaeoglobus fulgidus: Mechanisms of oligomerisation and thermal stabilisation

Journal of Molecular Biology

Volumn 335, Issue 1, 2004, Pages 343-356

  Irimia, Adriana ^a   Vellieux, Frédéric M D ^a   Madern, Dominique ^a   Zaccaï, Giuseppe ^a,b   Karshikoff, Andrey ^c   Tibbelin, Gudrun ^c   Ladenstein, Rudolf ^c   Lien, Torleiv ^d   Birkeland, Nils Kåre ^d  

^a INSTITUT DE BIOLOGIE STRUCTURALE   (France)

^b INSTITUT LAUE LANGEVIN   (France)

^c KAROLINSKA INSTITUTE   (Sweden)

^d UNIVERSITY OF BERGEN   (Norway)

Author keywords

Crystal structure; Hyperthermophile; Loop shortening; LDH like MalDH

Indexed keywords

BACTERIAL PROTEIN; HYDROGEN; LACTATE DEHYDROGENASE; MALATE DEHYDROGENASE; MALDH PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE; SOLVENT; TETRAMER; UNCLASSIFIED DRUG;

ADAPTATION; ARCHAEOGLOBUS FULGIDUS; ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME BINDING; GENE DELETION; HALOPHILIC BACTERIUM; HIGH TEMPERATURE; HYDROGEN BOND; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; THERMOSTABILITY; CHEMICAL STRUCTURE; CHEMISTRY; DIMERIZATION; ENZYME STABILITY; ENZYMOLOGY; PROTEIN CONFORMATION; STRUCTURAL HOMOLOGY; TEMPERATURE; X RAY CRYSTALLOGRAPHY;

ARCHAEA; ARCHAEOGLOBUS; ARCHAEOGLOBUS FULGIDUS; HOMO;

ARCHAEOGLOBUS FULGIDUS; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; ENZYME STABILITY; MALATE DEHYDROGENASE; MOLECULAR STRUCTURE; NAD; PROTEIN CONFORMATION; STRUCTURAL HOMOLOGY, PROTEIN; TEMPERATURE;

EID: 0345118104     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.10.054     Document Type: Article

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