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Volumn 9, Issue 5, 2001, Pages 439-450
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The crystal structure of E. Coli pantothenate synthetase confirms it as a member of the cytidylyltransferase superfamily
a,d b a a c a |
Author keywords
Adenylate intermediate; Hinge bending; Rossmann fold; Selenomethionine MAD experiment; Vitamin B5
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Indexed keywords
ADENOSINE TRIPHOSPHATE;
AMINO ACID TRANSFER RNA LIGASE;
CYTIDYLYLTRANSFERASE;
PANTOTHENATE SYNTHETASE;
PANTOTHENIC ACID;
PEPTIDE SYNTHASE;
RECOMBINANT ENZYME;
SELENOMETHIONINE;
TRANSFERASE;
UNCLASSIFIED DRUG;
AMINO TERMINAL SEQUENCE;
ARTICLE;
BINDING SITE;
CARBOXY TERMINAL SEQUENCE;
CRYSTAL STRUCTURE;
ENZYME ACTIVE SITE;
ENZYME BINDING;
ENZYME PURIFICATION;
ESCHERICHIA COLI;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN DOMAIN;
PROTEIN EXPRESSION;
PROTEIN FAMILY;
PROTEIN FOLDING;
STRUCTURE ANALYSIS;
ADENOSINE TRIPHOSPHATE;
CRYSTALLOGRAPHY, X-RAY;
DIMERIZATION;
ESCHERICHIA COLI;
GENE EXPRESSION;
PEPTIDE SYNTHASES;
PROTEIN STRUCTURE, SECONDARY;
SOLUTIONS;
SUBSTRATE SPECIFICITY;
BACTERIA (MICROORGANISMS);
ESCHERICHIA COLI;
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EID: 0034984196
PISSN: 09692126
EISSN: None
Source Type: Journal
DOI: 10.1016/S0969-2126(01)00604-9 Document Type: Article |
Times cited : (74)
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References (54)
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