The crystal structure of the bifunctional primase-helicase of bacteriophage T7 (Q27642620)

3

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author name string

Eric A Toth

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Ying Li

2

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Yifan Cheng

Asymmetric interactions of hexameric bacteriophage T7 DNA helicase with the 5'- and 3'-tails of the forked DNA substrate.

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publication date

November 2003

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published in

Molecular Cell

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volume

12

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issue

5

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page(s)

1113-23

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cites work

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Architecture of the replication complex and DNA loops at the fork generated by the bacteriophage t4 proteins

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Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution

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Complete nucleotide sequence of bacteriophage T7 DNA and the locations of T7 genetic elements

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Bacteriophage T7 helicase/primase proteins form rings around single-stranded DNA that suggest a general structure for hexameric helicases

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The linker region between the helicase and primase domains of the bacteriophage T7 gene 4 protein is critical for hexamer formation

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Structure of the gene 2.5 protein, a single-stranded DNA binding protein encoded by bacteriophage T7

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The 3′-tail of a forked-duplex sterically determines whether one or two DNA strands pass through the central channel of a replication-fork helicase 1 1Edited by M. Gottesman

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DNA is bound within the central hole to one or two of the six subunits of the T7 DNA helicase

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The Methanobacterium thermoautotrophicum MCM protein can form heptameric rings

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Trading places on DNA--a three-point switch underlies primer handoff from primase to the replicative DNA polymerase

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Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

14636571

1 reference

Consolidated OpenCitations Corpus – April 2017