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Structural insight into recruitment of translesion DNA polymerase Dpo4 to sliding clamp PCNA.

Abstract:

DNA polymerases are co-ordinated by sliding clamps (PCNA/beta-clamp) in translesion synthesis. It is unclear how these enzymes assemble on PCNA with geometric and functional compatibility. We report the crystal structure of a full-length Y-family polymerase, Dpo4, in complex with heterodimeric PCNA1-PCNA2 at 2.05 A resolution. Dpo4 exhibits an extended conformation that differs from the Dpo4 structures in apo- or DNA-bound form. Two hinges have been identified in Dpo4, which render the multid...

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Publication status:
Published

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Authors


Kirouac, K More by this author
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Institution:
University of Oxford
Department:
Oxford, MSD, Pathology Dunn School
Journal:
Molecular microbiology
Volume:
71
Issue:
3
Pages:
678-691
Publication date:
2009-02-05
DOI:
EISSN:
1365-2958
ISSN:
0950-382X
URN:
uuid:6a32b344-6e46-47d2-b0fe-59c8fee452ba
Source identifiers:
18238
Local pid:
pubs:18238

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