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Volumn 41, Issue 31, 2002, Pages 9863-9872
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Multicopy crystallographic refinement of a relaxed glutamine synthetase from Mycobacterium tuberculosis highlights flexible loops in the enzymatic mechanism and its regulation
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Author keywords
[No Author keywords available]
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Indexed keywords
FLEXIBLE LOOPS;
ADENOSINETRIPHOSPHATE;
CATALYSIS;
COMPUTER SIMULATION;
CRYSTAL STRUCTURE;
CRYSTALLOGRAPHY;
ENZYMES;
BIOCHEMISTRY;
ADENOSINE PHOSPHATE;
ADENOSINE TRIPHOSPHATE;
ASPARTIC ACID;
CITRIC ACID;
GLUTAMATE AMMONIA LIGASE;
GLUTAMIC ACID;
GLUTAMINE;
METAL ION;
TYROSINE;
ADENYLATION;
AMINO ACID SYNTHESIS;
ARTICLE;
ATOM;
BETA SHEET;
CATALYSIS;
CONFORMATIONAL TRANSITION;
CRYSTAL STRUCTURE;
CRYSTALLOGRAPHY;
ENZYME ACTIVE SITE;
ENZYME CONFORMATION;
ENZYME MECHANISM;
ENZYME REGULATION;
ENZYME SUBSTRATE COMPLEX;
METAL BINDING;
MODEL;
MOLECULAR DYNAMICS;
MYCOBACTERIUM TUBERCULOSIS;
NONHUMAN;
PRIORITY JOURNAL;
SALMONELLA TYPHIMURIUM;
CATALYSIS;
CRYSTALLOGRAPHY, X-RAY;
GLUTAMATE-AMMONIA LIGASE;
MODELS, MOLECULAR;
MYCOBACTERIUM TUBERCULOSIS;
PROTEIN CONFORMATION;
ACTINOBACTERIA (CLASS);
BACTERIA (MICROORGANISMS);
MYCOBACTERIUM;
MYCOBACTERIUM TUBERCULOSIS;
SALMONELLA TYPHIMURIUM;
UNCULTURED ACTINOMYCETE;
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EID: 0037031287
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi020254s Document Type: Article |
Times cited : (73)
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References (30)
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