Opening of a monomer-monomer interface of the trimeric bacteriophage T4-coded GP45 sliding clamp is required for clamp loading onto DNA

Proceedings of the National Academy of Sciences of the United States of America

Volumn 96, Issue 22, 1999, Pages 12448-12453

  Latham, Gary J ^a,b   Dong, Feng ^a,c   Pietroni, Paola ^a   Dozono, Jody M ^a   Bacheller, Daniel J ^a   Von Hippel, Peter H ^a  

^a UNIVERSITY OF OREGON   (United States)

^b ZymeTx Incorporated   (United States)

^c GEORGIA INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

ATP hydrolysis; Processivity clamp; Replication complex; Subunit crosslinking

Indexed keywords

ADENOSINE TRIPHOSPHATASE; DNA POLYMERASE; GLYCOPROTEIN; MONOMER; VIRUS PROTEIN;

ARTICLE; BACTERIOPHAGE T4; CONFORMATIONAL TRANSITION; CROSS LINKING; DNA REPLICATION; DNA SYNTHESIS; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL;

ADENOSINE TRIPHOSPHATASES; BACTERIOPHAGE T4; BIOPOLYMERS; CROSS-LINKING REAGENTS; DNA, VIRAL; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; TRANS-ACTIVATORS; VIRAL PROTEINS;

UNIDENTIFIED BACTERIOPHAGE;

EID: 0033607159     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.96.22.12448     Document Type: Article

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