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Volumn 9, Issue 6, 2002, Pages 447-452
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E. coli aconitase B structure reveals a HEAT-like domain with implications for protein-protein recognition
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Author keywords
[No Author keywords available]
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Indexed keywords
ACONITASE B;
ACONITATE HYDRATASE;
BACTERIAL ENZYME;
HEAT PROTEIN;
IRON;
SULFUR;
UNCLASSIFIED DRUG;
ARTICLE;
CATALYST;
CONTROLLED STUDY;
ENZYME ACTIVE SITE;
ENZYME STRUCTURE;
ESCHERICHIA COLI;
MOLECULAR RECOGNITION;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN DOMAIN;
PROTEIN FAMILY;
PROTEIN PROTEIN INTERACTION;
RNA BINDING;
TRANSCRIPTION REGULATION;
ACONITATE HYDRATASE;
AMINO ACID MOTIFS;
AMINO ACID SEQUENCE;
ANIMALS;
BINDING SITES;
CATTLE;
CONSERVED SEQUENCE;
CRYSTALLOGRAPHY, X-RAY;
ESCHERICHIA COLI;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
MULTIENZYME COMPLEXES;
PROTEIN BINDING;
PROTEIN STRUCTURE, TERTIARY;
RNA;
RNA-BINDING PROTEINS;
SEQUENCE ALIGNMENT;
STRUCTURE-ACTIVITY RELATIONSHIP;
BACTERIA (MICROORGANISMS);
ESCHERICHIA COLI;
NEGIBACTERIA;
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EID: 0036260715
PISSN: 10728368
EISSN: None
Source Type: Journal
DOI: 10.1038/nsb801 Document Type: Article |
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Times cited : (45)
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References (45)
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