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Volumn 8, Issue 8, 2000, Pages 883-895
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Crystal structures of substrate binding to Bacillus subtilis holo-(acyl carrier protein) synthase reveal a novel trimeric arrangement of molecules resulting in three active sites
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Author keywords
Acyl carrier protein; Coenzyme A; Fatty acid biosynthesis; Phosphopantetheinyl transferase; Three dimensional structure; X ray crystallography
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Indexed keywords
ACYL CARRIER PROTEIN;
ACYL CARRIER PROTEIN SYNTHETASE;
CARRIER PROTEIN;
COENZYME A;
TRANSFERASE;
UNCLASSIFIED DRUG;
ARTICLE;
BACILLUS SUBTILIS;
CATALYSIS;
COMPLEX FORMATION;
CRYSTAL STRUCTURE;
DIMERIZATION;
ENZYME ACTIVE SITE;
ENZYME ACTIVITY;
ENZYME BINDING;
ENZYME CONFORMATION;
FATTY ACID SYNTHESIS;
HYDROPHOBICITY;
NONHUMAN;
PRIORITY JOURNAL;
STRUCTURE ANALYSIS;
BACILLUS SUBTILIS;
BACTERIA (MICROORGANISMS);
POSIBACTERIA;
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EID: 0034662753
PISSN: 09692126
EISSN: None
Source Type: Journal
DOI: 10.1016/S0969-2126(00)00178-7 Document Type: Article |
Times cited : (205)
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References (42)
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