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Volumn 277, Issue 2, 2002, Pages 1553-1559
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The β-hairpin motif of UvrB is essential for DNA binding, damage processing, and UvrC-mediated incisions
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Author keywords
[No Author keywords available]
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Indexed keywords
ADENOSINETRIPHOSPHATE;
CRYSTAL STRUCTURE;
DNA;
MUTAGENESIS;
DAMAGE PROCESSING;
BIOCHEMISTRY;
ADENOSINE TRIPHOSPHATASE;
HELICASE;
NUCLEASE;
PROTEIN UVRB;
UNCLASSIFIED DRUG;
AMINO ACID SEQUENCE;
ARTICLE;
BACILLUS;
BACILLUS CALDOTENAX;
CONFORMATIONAL TRANSITION;
CRYSTAL STRUCTURE;
DELETION MUTANT;
DNA BINDING;
DNA DAMAGE;
DNA PROTEIN COMPLEX;
DNA SEQUENCE;
ENZYME ACTIVITY;
EXCISION REPAIR;
MOLECULAR MODEL;
MOLECULAR RECOGNITION;
PRIORITY JOURNAL;
PROTEIN FOLDING;
PROTEIN MOTIF;
PROTEIN PROCESSING;
ADENOSINE TRIPHOSPHATASES;
AMINO ACID MOTIFS;
BACILLUS;
BACTERIAL PROTEINS;
CIRCULAR DICHROISM;
DNA;
DNA HELICASES;
DNA REPAIR;
DNA-BINDING PROTEINS;
ENDODEOXYRIBONUCLEASES;
ESCHERICHIA COLI PROTEINS;
MOLECULAR STRUCTURE;
PROTEIN STRUCTURE, SECONDARY;
PROTEIN SUBUNITS;
BACILLUS CALDOTENAX;
CHEN;
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EID: 0037059785
PISSN: 00219258
EISSN: None
Source Type: Journal
DOI: 10.1074/jbc.M108847200 Document Type: Article |
Times cited : (91)
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References (38)
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