Crystal structure of MabA from Mycobacterium tuberculosis, a reductase involved in long-chain fatty acid biosynthesis

Journal of Molecular Biology

Volumn 320, Issue 2, 2002, Pages 249-261

  Cohen Gonsaud, Martin ^a,b   Ducasse, Stéphanie ^c   Hoh, Francois ^a   Zerbib, Didier ^c   Labesse, Gilles ^a   Quemard, Annaïk ^c  

^a CENTRE DE BIOCHIMIE STRUCTURALE   (France)

^b BioXTal   (France)

^c INSTITUT DE PHARMACOLOGIE ET DE BIOLOGIE STRUCTURALE   (France)

Author keywords

Activation; Conformational change; Enzymatic activity; Molecular replacement; ketoacyl reductase

Indexed keywords

CARRIER PROTEIN; ENZYME INHIBITOR; HYDROLYASE; ISONIAZID; LONG CHAIN FATTY ACID; MYCOLIC ACID; OXIDOREDUCTASE; PROTEIN; PROTEIN FABG1; PROTEIN INHA; PROTEIN MABA; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; TRYPTOPHAN; TUBERCULOSTATIC AGENT; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL MEMBRANE; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME INHIBITION; ENZYME STRUCTURE; ESCHERICHIA COLI; FATTY ACID SYNTHESIS; FLUORESCENCE SPECTROSCOPY; MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; REDUCTION; SPECIES DIFFERENCE;

CORYNEBACTERINEAE; ESCHERICHIA COLI; MYCOBACTERIUM; MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS;

EID: 0036299101     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)00463-1     Document Type: Article

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