Three-Dimensional Structures of Apo- and Holo-l-Alanine Dehydrogenase from Mycobacterium tuberculosis Reveal Conformational Changes upon Coenzyme Binding

Journal of Molecular Biology

Volumn 377, Issue 4, 2008, Pages 1161-1173

  Ågren, Daniel ^a   Stehr, Matthias ^b   Berthold, Catrine L ^a   Kapoor, Shobhna ^b   Oehlmann, Wulf ^c   Singh, Mahavir ^b,c   Schneider, Gunter ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

^b HELMHOLTZ CENTRE FOR INFECTION RESEARCH   (Germany)

^c LIONEX DIAGNOSTICS AND THERAPEUTICS GMBH   (Germany)

Author keywords

enzyme mechanism; persistent tuberculosis; protein structure; ternary complex; X ray crystallography

Indexed keywords

ALANINE DEHYDROGENASE; AMINO ACID; CARBON; DINUCLEOTIDE; MUTANT PROTEIN; NICOTINAMIDE; PROTEIN SUBUNIT; PYRUVIC ACID;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME BINDING; ENZYME LOCALIZATION; ENZYME STABILITY; ENZYME STRUCTURE; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; SITE DIRECTED MUTAGENESIS;

MYCOBACTERIUM TUBERCULOSIS;

EID: 40849117861     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.01.091     Document Type: Article

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