Summary information and primary citation

PDB-id
2qby; SNAP-derived features in text and JSON formats; DNAproDB
Class
replication-DNA
Method
X-ray (3.35 Å)
Summary
Crystal structure of a heterodimer of cdc6-orc1 initiators bound to origin DNA (from s. solfataricus)
Reference
Dueber EL, Corn JE, Bell SD, Berger JM (2007): "Replication origin recognition and deformation by a heterodimeric archaeal Orc1 complex." Science, 317, 1210-1213. doi: 10.1126/science.1143690.
Abstract
The faithful duplication of genetic material depends on essential DNA replication initiation factors. Cellular initiators form higher-order assemblies on replication origins, using adenosine triphosphate (ATP) to locally remodel duplex DNA and facilitate proper loading of synthetic replisomal components. To better understand initiator function, we determined the 3.4 angstrom-resolution structure of an archaeal Cdc6/Orc1 heterodimer bound to origin DNA. The structure demonstrates that, in addition to conventional DNA binding elements, initiators use their AAA+ ATPase domains to recognize origin DNA. Together these interactions establish the polarity of initiator assembly on the origin and induce substantial distortions into origin DNA strands. Biochemical and comparative analyses indicate that AAA+/DNA contacts observed in the structure are dynamic and evolutionarily conserved, suggesting that the complex forms a core component of the basal initiation machinery.

Cartoon-block schematics in six views (download the tarball)

PyMOL session file Download PDB file View in 3Dmol.js