Mechanism of DnaB helicase of Escherichia coli: Structural domains involved in ATP hydrolysis, DNA binding, and oligomerization

Biochemistry

Volumn 38, Issue 34, 1999, Pages 10919-10928

  Biswas, Esther E ^a,b   Biswas, Subhasis B ^a  

^a UMDNJ School of Osteopathic Medicine   (United States)

^b UNIVERSITY OF MEDICINE AND DENTISTRY OF NEW JERSEY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; HELICASE; MUTANT PROTEIN;

AMINO ACID COMPOSITION; ARTICLE; CARBOXY TERMINAL SEQUENCE; DIMERIZATION; DNA BINDING; ENERGY TRANSFER; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME MECHANISM; ESCHERICHIA COLI; HYDROLYSIS; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN QUATERNARY STRUCTURE; STRUCTURE ACTIVITY RELATION;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEINS; DNA HELICASES; DNA, SINGLE-STRANDED; DNA-BINDING PROTEINS; DNAB HELICASES; ESCHERICHIA COLI; GENE DELETION; GENES, BACTERIAL; HYDROLYSIS; MAGNESIUM; PEPTIDE FRAGMENTS; PLASMIDS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP;

ESCHERICHIA COLI;

EID: 0033600551     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi990048t     Document Type: Article

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