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-Structure paper
Title | Nucleotide-dependent conformational changes in the DnaA-like core of the origin recognition complex. |
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Journal, issue, pages | Nat Struct Mol Biol, Vol. 13, Issue 8, Page 684-690, Year 2006 |
Publish date | Jul 9, 2006 |
Authors | Megan G Clarey / Jan P Erzberger / Patricia Grob / Andres E Leschziner / James M Berger / Eva Nogales / Michael Botchan / |
PubMed Abstract | 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. |
External links | Nat Struct Mol Biol / PubMed:16829958 |
Methods | EM (single particle) |
Resolution | 34.0 Å |
Structure data | EMDB-1252: EMDB-1253: |
Source |
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