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Volumn 9, Issue 12, 2001, Pages 1153-1164
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The 1.6 Å crystal structure of E. coli Argininosuccinate synthetase suggests a conformational change during catalysis
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Author keywords
"N type" ATP pyrophosphatase; Argininosuccinate synthetase; Conformational change; Mutation analysis; Structure; Urea cycle
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Indexed keywords
ADENOSINE TRIPHOSPHATE;
ARGININOSUCCINATE SYNTHASE;
ASPARTIC ACID;
CITRULLINE;
INORGANIC PYROPHOSPHATASE;
SELENOMETHIONINE;
NUCLEOTIDE;
AMINO ACID SEQUENCE;
ARTICLE;
CATALYSIS;
CONFORMATIONAL TRANSITION;
CONTROLLED STUDY;
CRYSTAL STRUCTURE;
ENZYME CONFORMATION;
ENZYME PURIFICATION;
ENZYME STRUCTURE;
ENZYME SUBSTRATE;
ESCHERICHIA COLI;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN BINDING;
PROTEIN DOMAIN;
PROTEIN EXPRESSION;
PROTEIN LOCALIZATION;
SEQUENCE HOMOLOGY;
ANIMAL;
BINDING SITE;
CHEMICAL MODEL;
CHEMICAL STRUCTURE;
CHEMISTRY;
DIMERIZATION;
ENZYMOLOGY;
GENETICS;
HUMAN;
METABOLISM;
MOLECULAR GENETICS;
MUTATION;
PROTEIN CONFORMATION;
PROTEIN SECONDARY STRUCTURE;
PROTEIN TERTIARY STRUCTURE;
X RAY CRYSTALLOGRAPHY;
BACTERIA (MICROORGANISMS);
ESCHERICHIA COLI;
MAMMALIA;
NEGIBACTERIA;
ADENOSINE TRIPHOSPHATE;
AMINO ACID SEQUENCE;
ANIMAL;
ARGININOSUCCINATE SYNTHASE;
ASPARTIC ACID;
BINDING SITES;
CATALYSIS;
CITRULLINE;
CRYSTALLOGRAPHY, X-RAY;
DIMERIZATION;
ESCHERICHIA COLI;
HUMAN;
MODELS, CHEMICAL;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
MUTATION;
NUCLEOTIDES;
PROTEIN CONFORMATION;
PROTEIN STRUCTURE, SECONDARY;
PROTEIN STRUCTURE, TERTIARY;
SEQUENCE HOMOLOGY, AMINO ACID;
SUPPORT, NON-U.S. GOV'T;
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EID: 0035653365
PISSN: 09692126
EISSN: None
Source Type: Journal
DOI: 10.1016/S0969-2126(01)00683-9 Document Type: Article |
Times cited : (33)
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References (54)
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