Bacteriophage T4 gene 59 helicase assembly protein binds replication fork DNA. The 1.45 Å resolution crystal structure reveals a novel α-helical two-domain fold

Journal of Molecular Biology

Volumn 296, Issue 2, 2000, Pages 597-612

  Mueser, Timothy C ^a   Jones, Charles E ^b   Nossal, Nancy G ^b   Hyde, C Craig ^a  

^a NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES   (United States)

^b NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

Author keywords

DNA replication; Fork DNA binding; Helicase; Helicase assembly factor; HMG domain

Indexed keywords

DNA; DNA BINDING PROTEIN; HELICASE ASSEMBLY PROTEIN; PROTEIN T4 GENE 59; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; BACTERIOPHAGE T4; BINDING AFFINITY; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CRYSTAL STRUCTURE; DNA REPLICATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DNA BINDING; PROTEIN DNA INTERACTION; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

EID: 0034681291     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3438     Document Type: Article

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