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-Structure paper
タイトル | Nucleotide-dependent conformational changes in the DnaA-like core of the origin recognition complex. |
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ジャーナル・号・ページ | Nat Struct Mol Biol, Vol. 13, Issue 8, Page 684-690, Year 2006 |
掲載日 | 2006年7月9日 |
著者 | Megan G Clarey / Jan P Erzberger / Patricia Grob / Andres E Leschziner / James M Berger / Eva Nogales / Michael Botchan / |
PubMed 要旨 | Structural details of initiator proteins for DNA replication have provided clues to the molecular events in this process. EM reconstructions of the Drosophila melanogaster origin recognition complex ...Structural details of initiator proteins for DNA replication have provided clues to the molecular events in this process. EM reconstructions of the Drosophila melanogaster origin recognition complex (ORC) reveal nucleotide-dependent conformational changes in the core of the complex. All five AAA+ domains in ORC contain a conserved structural element that, in DnaA, promotes formation of a right-handed helix, indicating that helical AAA+ substructures may be a feature of all initiators. A DnaA helical pentamer can be docked into ORC, and the location of Orc5 uniquely positions this core. The results suggest that ATP-dependent conformational changes observed in ORC derive from reorientation of the AAA+ domains. By analogy to the DNA-wrapping activity of DnaA, we posit that ORC together with Cdc6 prepares origin DNA for helicase loading through mechanisms related to the established pathway of prokaryotes. |
リンク | Nat Struct Mol Biol / PubMed:16829958 |
手法 | EM (単粒子) |
解像度 | 34.0 Å |
構造データ | EMDB-1252: EMDB-1253: |
由来 |
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