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- Publisher
- Wiley
- Copyright
- Copyright © 2006 Wiley Subscription Services, Inc., A Wiley Company
- ISSN
- 1744-3091
- eISSN
- 1744-3091
- DOI
- 10.1107/S1744309106004362
- pmid
- 16511315
- Publisher site
- See Article on Publisher Site
Abstract
Replicative DNA polymerase interacts with processivity factors, the β‐subunit of DNA polymerase III or proliferating cell nuclear antigen (PCNA), in order to function with a long template DNA. The archaeal replicative DNA polymerase from Pyrococcus furiosus interacts with PCNA via its PCNA‐interacting protein (PIP) motif at the C‐terminus. The PCNA homotrimeric ring contains one PIP interacting site on each monomer and since the ring can accommodate up to three molecules simultaneously, formation of a stable stoichiometric complex of PCNA with its interacting protein has been difficult to control in vitro. A stable complex of the DNA polymerase with PCNA, using a PCNA monomer mutant, has been purified and crystallized. The best ordered crystal diffracted to 3.0 Å resolution using synchrotron radiation. The crystals belong to space group P21212, with unit‐cell parameters a = 225.3, b = 123.3, c = 91.3 Å.
Journal
Acta Crystallographica Section F – Wiley
Published: Mar 1, 2006