Interplay of Clamp Loader Subunits in Opening the β Sliding Clamp of Escherichia coli DNA Polymerase III Holoenzyme

Journal of Biological Chemistry

Volumn 276, Issue 50, 2001, Pages 47185-47194

  Leu, Frank P ^a   O'Donnell, Mike ^b  

^a Weill Cornell Medical Center   (United States)

^b ROCKEFELLER UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIGENS; CELLS; DNA; ESCHERICHIA COLI; PROTEINS;

DIMER INTERFACES;

BIOCHEMISTRY;

ADENOSINE TRIPHOSPHATE; BETA DIMER; CYCLINE; DELTA CHAIN; DIMER; DNA; DNA POLYMERASE; DNA POLYMERASE 3 HOLOENZYME; GAMMA CHAIN; PROTEIN SUBUNIT; REPLICATION FACTOR C; RNA DIRECTED RNA POLYMERASE; UNCLASSIFIED DRUG; ACTIVATOR 1 PROTEIN; DNA BINDING PROTEIN; DNA BINDING PROTEINS; DNA DIRECTED DNA POLYMERASE GAMMA; HOLOENZYME;

ANIMAL CELL; ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; DNA BINDING; ENZYME STRUCTURE; ENZYME SUBUNIT; ESCHERICHIA COLI; EUKARYOTE; GAMMA COMPLEX CLAMP LOADER; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; REACTION ANALYSIS; RING CLOSING METATHESIS; RING OPENING; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS; BIOLOGICAL MODEL; CATALYSIS; CHEMISTRY; DIMERIZATION; DOSE RESPONSE; ENZYMOLOGY; METABOLISM; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN MOTIF; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SURFACE PLASMON RESONANCE; TIME; X RAY CRYSTALLOGRAPHY;

ANIMALIA; ESCHERICHIA COLI; EUKARYOTA; NEGIBACTERIA;

ADENOSINE TRIPHOSPHATE; AMINO ACID MOTIFS; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; DNA; DNA POLYMERASE III; DNA-BINDING PROTEINS; DOSE-RESPONSE RELATIONSHIP, DRUG; ESCHERICHIA COLI; HOLOENZYMES; MODELS, BIOLOGICAL; PROLIFERATING CELL NUCLEAR ANTIGEN; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SUPPORT, NON-U.S. GOV'T; SUPPORT, U.S. GOV'T, P.H.S.; SURFACE PLASMON RESONANCE; TIME FACTORS;

EID: 0035861654     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M106780200     Document Type: Article

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