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Updated: Aug 4, 2026

Analyzing and Building Nucleic Acid Structures with 3DNA
Published on: April 26, 2013
Nucleotide-dependent conformational changes in the DnaA-like core of the origin recognition complex
Megan G Clarey1, Jan P Erzberger, Patricia Grob
1Division of Biochemistry & Molecular Biology, Molecular & Cell Biology Department, 1 Barker Hall, University of California, Berkeley, California 94720, USA.
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 (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.
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