The crystal structure of Mycobacterium tuberculosis adenylate kinase in complex with two molecules of ADP and Mg2+ supports an associative mechanism for phosphoryl transfer

Protein Science

Volumn 15, Issue 6, 2006, Pages 1489-1493

  Bellinzoni, Marco ^a   Haouz, Ahmed ^b   Graña, Martin ^a   Munier Lehmann, Hélène ^a   Shepard, William ^c   Alzari, Pedro M ^a,b  

^a INSTITUT PASTEUR   (France)

^b CNRS   (France)

^c SYNCHROTRON SOLEIL   (France)

Author keywords

Adenylate kinase; Associative mechanism; Mycobacterium tuberculosis; Phosphoryl transfer; X ray crystallography

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENYLATE KINASE; MAGNESIUM;

ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; ENZYME STRUCTURE; MYCOBACTERIUM TUBERCULOSIS; PRIORITY JOURNAL; PROTEIN CONFORMATION; STRUCTURE ANALYSIS; X RAY CRYSTALLOGRAPHY;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ADENYLATE KINASE; BINDING SITES; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; MAGNESIUM; MODELS, MOLECULAR; MYCOBACTERIUM TUBERCULOSIS; PROTEIN CONFORMATION;

MYCOBACTERIUM TUBERCULOSIS;

EID: 33744501841     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.062163406     Document Type: Article

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