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TitleMechanism of replication machinery assembly as revealed by the DNA ligase-PCNA-DNA complex architecture.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 106, Issue 12, Page 4647-4652, Year 2009
Publish dateMar 24, 2009
AuthorsKouta Mayanagi / Shinichi Kiyonari / Mihoko Saito / Tsuyoshi Shirai / Yoshizumi Ishino / Kosuke Morikawa /
PubMed AbstractThe 3D structure of the ternary complex, consisting of DNA ligase, the proliferating cell nuclear antigen (PCNA) clamp, and DNA, was investigated by single-particle analysis. This report presents the ...The 3D structure of the ternary complex, consisting of DNA ligase, the proliferating cell nuclear antigen (PCNA) clamp, and DNA, was investigated by single-particle analysis. This report presents the structural view, where the crescent-shaped DNA ligase with 3 distinct domains surrounds the central DNA duplex, encircled by the closed PCNA ring, thus forming a double-layer structure with dual contacts between the 2 proteins. The relative orientations of the DNA ligase domains, which remarkably differ from those of the known crystal structures, suggest that a large domain rearrangement occurs upon ternary complex formation. A second contact was found between the PCNA ring and the middle adenylation domain of the DNA ligase. Notably, the map revealed a substantial DNA tilt from the PCNA ring axis. This structure allows us to propose a switching mechanism for the replication factors operating on the PCNA ring.
External linksProc Natl Acad Sci U S A / PubMed:19255439 / PubMed Central
MethodsEM (single particle)
Resolution17.0 Å
Structure data

EMDB-1485:
The archaeal DNA Ligase-PCNA-DNA complex
Method: EM (single particle) / Resolution: 17.0 Å

Source
  • Pyrococcus furiosus (archaea)
  • synthetic construct (others)

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