Mycobacterium tuberculosis thymidylate kinase: Structural studies of intermediates along the reaction pathway

Journal of Molecular Biology

Volumn 327, Issue 5, 2003, Pages 1077-1092

  Fioravanti, E ^a,b   Haouz, A ^c   Ursby, T ^a,b,d   Munier Lehmann, H ^c   Delarue, M ^c   Bourgeois, D ^a,b  

^a INSTITUT DE BIOLOGIE STRUCTURALE   (France)

^b EUROPEAN SYNCHROTRON RADIATION FACILITY   (France)

^c INSTITUT PASTEUR   (France)

^d LUND UNIVERSITY   (Sweden)

Author keywords

Catalytic mechanism; Conformational change; Crystal structure; Mycobacterium tuberculosis; Thymidylate kinase

Indexed keywords

ANION; ARGININE; BACTERIAL ENZYME; ENZYME INHIBITOR; HYDROXYL GROUP; MAGNESIUM ION; METAL; METAL ION; NUCLEOSIDE MONOPHOSPHATE KINASE; NUCLEOSIDE TRIPHOSPHATE; THYMIDINE DIPHOSPHATE; THYMIDINE PHOSPHATE; THYMIDINE TRIPHOSPHATE; THYMIDYLATE KINASE; UNCLASSIFIED DRUG; WATER;

ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; DRUG DESIGN; ELECTRICITY; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME INHIBITION; ENZYME MECHANISM; ENZYME PHOSPHORYLATION; ENZYME REGULATION; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; FEEDBACK SYSTEM; METAL BINDING; MYCOBACTERIUM TUBERCULOSIS; PRIORITY JOURNAL;

MYCOBACTERIUM; MYCOBACTERIUM TUBERCULOSIS;

EID: 0344837328     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00202-X     Document Type: Article

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