Unusual structural features of hydantoin lesions translate into efficient recognition by Escherichia coli Fpg

Biochemistry

Volumn 46, Issue 33, 2007, Pages 9355-9365

  Krishnamurthy, Nirmala ^b   Muller, James G ^b   Burrows, Cynthia J ^b   David, Sheila S ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF UTAH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DNA REPLICATION; HYDANTOIN LESIONS; MUTAGENIC POTENTIALS;

DNA; ENZYMES; ESCHERICHIA COLI; IRON COMPOUNDS; MUTAGENESIS; NUCLEOTIDES;

CRYSTALLINE MATERIALS;

8 HYDROXYGUANINE; BACTERIAL PROTEIN; DNA; DNA GLYCOSYLTRANSFERASE; EDETIC ACID; FERROUS ION; GUANIDINOHYDANTOIN; GUANINE; HYDANTOIN DERIVATIVE; METHIDIUM PROPYL EDETIC ACID; PROTEIN E3Q ECFPG; PROTEIN ECFPG; REACTIVE OXYGEN METABOLITE; SPIROIMINODIHYDANTOIN; UNCLASSIFIED DRUG;

ARTICLE; BASE PAIRING; BINDING AFFINITY; BINDING SITE; DNA BINDING; DNA FOOTPRINTING; DNA REPLICATION; ENZYME STRUCTURE; ESCHERICHIA COLI; EXCISION REPAIR; IN VIVO STUDY; INTERCALATION COMPLEX; MOLECULAR RECOGNITION; MUTAGENESIS; NONHUMAN; OXIDATION KINETICS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

BASE PAIRING; BASE SEQUENCE; CATALYSIS; DNA; DNA REPAIR; DNA-FORMAMIDOPYRIMIDINE GLYCOSYLASE; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GUANIDINES; GUANOSINE; HYDANTOINS; SPIRO COMPOUNDS;

ESCHERICHIA COLI;

EID: 34548085699     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi602459v     Document Type: Article

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