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TitleCdc6-induced conformational changes in ORC bound to origin DNA revealed by cryo-electron microscopy.
Journal, issue, pagesStructure, Vol. 20, Issue 3, Page 534-544, Year 2012
Publish dateMar 7, 2012
AuthorsJingchuan Sun / Hironori Kawakami / Juergen Zech / Christian Speck / Bruce Stillman / Huilin Li /
PubMed AbstractThe eukaryotic origin recognition complex (ORC) interacts with and remodels origins of DNA replication prior to initiation in S phase. Here, we report a single-particle cryo-EM-derived structure of ...The eukaryotic origin recognition complex (ORC) interacts with and remodels origins of DNA replication prior to initiation in S phase. Here, we report a single-particle cryo-EM-derived structure of the supramolecular assembly comprising Saccharomyces cerevisiae ORC, the replication initiation factor Cdc6, and double-stranded ARS1 origin DNA in the presence of ATPγS. The six subunits of ORC are arranged as Orc1:Orc4:Orc5:Orc2:Orc3, with Orc6 binding to Orc2. Cdc6 binding changes the conformation of ORC, in particular reorienting the Orc1 N-terminal BAH domain. Segmentation of the 3D map of ORC-Cdc6 on DNA and docking with the crystal structure of the homologous archaeal Orc1/Cdc6 protein suggest an origin DNA binding model in which the DNA tracks along the interior surface of the crescent-like ORC. Thus, ORC bends and wraps the DNA. This model is consistent with the observation that binding of a single Cdc6 extends the ORC footprint on origin DNA from both ends.
External linksStructure / PubMed:22405012 / PubMed Central
MethodsEM (single particle)
Resolution15.0 Å
Structure data

EMDB-5381:
Cdc6-induced Conformational Changes in ORC Bound To Origin DNA Revealed by Cryo-Electron Microscopy. This map may be mirrored (based on comparison to EMD-5625).
Method: EM (single particle) / Resolution: 15.0 Å

Source
  • Saccharomyces cerevisiae (brewer's yeast)

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