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Volumn 5, Issue 10, 2000, Pages 803-813
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Two basic residues, Lys- 107 and Lys-118, of RuvC resolvase are involved in critical contacts with the Holliday junction for its resolution
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Author keywords
[No Author keywords available]
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Indexed keywords
DIVALENT CATION;
DNA;
LYSINE;
MAGNESIUM ION;
MANGANESE;
RESOLVASE;
RIBONUCLEASE;
SODIUM CHLORIDE;
ARTICLE;
CATALYSIS;
CONTROLLED STUDY;
CRYSTALLOGRAPHY;
DNA BINDING;
ENZYME ACTIVE SITE;
ESCHERICHIA COLI;
GENE MUTATION;
HOLLIDAY JUNCTION;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN ANALYSIS;
PROTEIN DNA BINDING;
PROTEIN INTERACTION;
PROTEIN PURIFICATION;
AMINO ACID SEQUENCE;
BACTERIAL PROTEINS;
CATALYTIC DOMAIN;
DNA REPAIR;
DNA, BACTERIAL;
ENDODEOXYRIBONUCLEASES;
ESCHERICHIA COLI;
ESCHERICHIA COLI PROTEINS;
LYSINE;
MAGNESIUM;
MANGANESE;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
MUTATION;
PROTEIN CONFORMATION;
SEQUENCE ALIGNMENT;
SODIUM CHLORIDE;
TEMPERATURE;
ESCHERICHIA COLI;
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EID: 0033766466
PISSN: 13569597
EISSN: None
Source Type: Journal
DOI: 10.1046/j.1365-2443.2000.00371.x Document Type: Article |
Times cited : (11)
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References (29)
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