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-Structure paper
タイトル | Cdc6-induced conformational changes in ORC bound to origin DNA revealed by cryo-electron microscopy. |
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ジャーナル・号・ページ | Structure, Vol. 20, Issue 3, Page 534-544, Year 2012 |
掲載日 | 2012年3月7日 |
著者 | Jingchuan Sun / Hironori Kawakami / Juergen Zech / Christian Speck / Bruce Stillman / Huilin Li / |
PubMed 要旨 | 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 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. |
リンク | Structure / PubMed:22405012 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 15.0 Å |
構造データ | EMDB-5381: |
由来 |
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