Structural and Dynamic Studies on Ligand-Free Adenylate Kinase from Mycobacterium tuberculosis Revealed a Closed Conformation that Can Be Related to the Reduced Catalytic Activity

Biochemistry

Volumn 43, Issue 1, 2004, Pages 67-77

  Miron, Simona ^a   Munier Lehmann, Hélène ^b   Craescu, Constantin T ^a  

^a INSTITUT CURIE   (France)

^b INSTITUT PASTEUR   (France)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; BIOSYNTHESIS; CATALYST ACTIVITY; CONFORMATIONS; CRYSTALLOGRAPHY; DISEASES; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; SIMULATED ANNEALING;

EUKARYOTES; TUBERCULOSIS;

ENZYMES;

ADENOSINE TRIPHOSPHATE; ADENYLATE KINASE; BACTERIAL ENZYME; CARBON 13; NITROGEN 15; PROTON;

ARTICLE; CATALYSIS; ENERGY METABOLISM; ENZYME ACTIVITY; ENZYME STRUCTURE; ESCHERICHIA COLI; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; STRUCTURE ANALYSIS; TUBERCULOSIS;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; EUKARYOTA; MYCOBACTERIUM; MYCOBACTERIUM TUBERCULOSIS;

EID: 0347357932     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0355995     Document Type: Article

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