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Volumn 40, Issue 13, 2001, Pages 3900-3911
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Structure of intact AhpF reveals a mirrored thioredoxin-like active site and implies large domain rotations during catalysis
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Author keywords
[No Author keywords available]
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Indexed keywords
LARGE DOMAIN ROTATIONS;
CATALYSIS;
CHEMICAL BONDS;
ENZYMES;
ESCHERICHIA COLI;
REDOX REACTIONS;
SUBSTRATES;
DIMERS;
FLAVOPROTEIN;
PROTEIN AHPF;
PROTEIN DISULFIDE REDUCTASE (GLUTATHIONE);
THIOREDOXIN REDUCTASE;
UNCLASSIFIED DRUG;
ARTICLE;
CATALYSIS;
ELECTRON TRANSPORT;
ENZYME ACTIVE SITE;
ENZYME STRUCTURE;
ENZYME SUBSTRATE;
ESCHERICHIA COLI;
HYDROGEN BOND;
MOLECULAR MODEL;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN DOMAIN;
PROTEIN FOLDING;
PYROCOCCUS FURIOSUS;
SALMONELLA TYPHIMURIUM;
AMINO ACID SEQUENCE;
BINDING SITES;
CATALYSIS;
COMPUTER SIMULATION;
CRYSTALLIZATION;
CRYSTALLOGRAPHY, X-RAY;
DIMERIZATION;
ESCHERICHIA COLI;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
PEPTIDE FRAGMENTS;
PEROXIDASES;
PROTEIN CONFORMATION;
PROTEIN STRUCTURE, SECONDARY;
PROTEIN STRUCTURE, TERTIARY;
SALMONELLA TYPHIMURIUM;
SEQUENCE HOMOLOGY, AMINO ACID;
THERMODYNAMICS;
THIOREDOXIN;
THIOREDOXIN REDUCTASE (NADPH);
ESCHERICHIA COLI;
PYROCOCCUS FURIOSUS;
SALMONELLA TYPHIMURIUM;
TYPHIMURIUM;
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EID: 0035799315
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi002765p Document Type: Article |
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Times cited : (49)
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References (51)
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