- 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...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1111/j.1365-2958.2008.06553.x
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- 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
- Language:
- English
- Keywords:
- Copyright date:
- 2009
Journal article
Structural insight into recruitment of translesion DNA polymerase Dpo4 to sliding clamp PCNA.
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