Crystal structure of shikimate kinase from Mycobacterium tuberculosis reveals the dynamic role of the LID domain in catalysis

Journal of Molecular Biology

Volumn 319, Issue 3, 2002, Pages 779-789

  Gu, Yijun ^a,b   Reshetnikova, Ludmila ^a   Li, Yue ^c   Wu, Yan ^c   Yan, Honggao ^c   Singh, Shivendra ^b   Ji, Xinhua ^a  

^a NATIONAL CANCER INSTITUTE   (United States)

^b UNIVERSITY OF PITTSBURGH CANCER INSTITUTE   (United States)

^c Michigan State University   (United States)

Author keywords

Drug design; Phosphoryl transfer; Shikimate kinase; Shikimate pathway; X ray crystallography

Indexed keywords

ADENINE; ADENOSINE DIPHOSPHATE; ADENOSINE DIPHOSPHATE MAGNESIUM; ARGININE; GUANIDINE; MAGNESIUM DERIVATIVE; PROLINE; SHIKIMIC ACID; UNCLASSIFIED DRUG;

ALPHA HELIX; ARTICLE; CATALYSIS; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; DRUG DESIGN; HYDROGEN BOND; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING;

ERWINIA; ERWINIA CHRYSANTHEMI; MAMMALIA; MYCOBACTERIUM; MYCOBACTERIUM TUBERCULOSIS;

EID: 0036300993     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)00339-X     Document Type: Article

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