Crystal structure of T7 gene 4 ring indicates a mechanism for sequential hydrolysis of nucleotides

Cell

Volumn 101, Issue 6, 2000, Pages 589-600

  Singleton, Martin R ^a   Sawaya, Michael R ^b   Ellenberger, Tom ^b   Wigley, Dale B ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b HARVARD MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE DERIVATIVE; DNA; HELICASE; NUCLEOTIDE;

ARTICLE; BACTERIOPHAGE; BINDING AFFINITY; BINDING SITE; CATALYSIS; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; GENE; GENE TRANSLOCATION; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL;

EID: 0034625236     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)80871-5     Document Type: Article

References (54)

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16. An N-terminal fragment of the gene 4 helicase/primase of bacteriophage T7 retains primase activity ion the absence of helicase activity
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37. 2+
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46. Structure of the RecA protein-ADP complex
47. Crystal structure of a DExx box helicase
48. Crystal structures of complexes of PcrA helicase with a DNA substrate indicate an inchworm mechanism
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50. Signal transduction via ras
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