The primase active site is on the outside of the hexameric bacteriophage T7 gene 4 helicase-primase ring

Journal of Molecular Biology

Volumn 311, Issue 5, 2001, Pages 951-956

  VanLoock, Margaret S ^a   Chen, Yen Ju ^a   Yu, Xiong ^a   Patel, Smita S ^b   Egelman, Edward H ^a  

^a UNIVERSITY OF VIRGINIA   (United States)

^b ROBERT WOOD JOHNSON UNIVERSITY HOSPITAL   (United States)

Author keywords

Electron microscopy; Image analysis; Molecular modeling; Protein DNA complexes; Ring proteins

Indexed keywords

DNA POLYMERASE; DNA PRIMASE; DOUBLE STRANDED DNA; HELICASE; OLIGORIBONUCLEOTIDE; PROTEIN; RNA; RNA POLYMERASE; THYMIDINE TRIPHOSPHATE;

ARTICLE; BACTERIOPHAGE; CRYSTAL STRUCTURE; DNA PROTEIN COMPLEX; ELECTRON MICROSCOPY; ENZYME ACTIVE SITE; ESCHERICHIA COLI; GENE; IMAGE ANALYSIS; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL;

ESCHERICHIA COLI;

EID: 0035979798     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2001.4932     Document Type: Article

References (35)

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27. Terminal regions of flagellin are disordered in solution
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