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Volumn 44, Issue 3, 2001, Pages 304-311
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The crystal structure of chorismate lyase shows a new fold and a tightly retained product
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Author keywords
Diffraction; Folding; Hydroxybenzoate; Product inhibition; Topology; Ubiquinone
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Indexed keywords
CHORISMIC ACID;
HELIX LOOP HELIX PROTEIN;
HYDROXYBENZOIC ACID;
LYASE;
UBIQUINONE;
AMINO ACID SEQUENCE;
ARTICLE;
CRYSTAL STRUCTURE;
CRYSTALLOGRAPHY;
DIFFRACTION;
ENZYME ACTIVE SITE;
ENZYME STRUCTURE;
ESCHERICHIA COLI;
HYDROPHOBICITY;
MOLECULAR MODEL;
PRIORITY JOURNAL;
PROTEIN BINDING;
PROTEIN FOLDING;
AMINO ACID SEQUENCE;
AMINO ACID SUBSTITUTION;
CRYSTALLIZATION;
ESCHERICHIA COLI;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
MUTATION;
OXO-ACID-LYASES;
PROTEIN CONFORMATION;
PROTEIN FOLDING;
SEQUENCE HOMOLOGY, AMINO ACID;
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EID: 0035882556
PISSN: 08873585
EISSN: None
Source Type: Journal
DOI: 10.1002/prot.1095 Document Type: Article |
Times cited : (33)
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References (27)
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