2QBY

Crystal structure of a heterodimer of Cdc6/Orc1 initiators bound to origin DNA (from S. solfataricus)

Summary for 2QBY

• Entry DOI: 10.2210/pdb2qby/pdb
• Descriptor: DNA (33-MER), Cell division control protein 6 homolog 1, Cell division control protein 6 homolog 3, ... (9 entities in total)
• Functional Keywords: winged-helix domain, helix-turn-helix, aaa+ atpase domain, protein-dna complex, double helix, replication-dna complex, replication/dna
• Biological source: Sulfolobus solfataricus; More
• Total number of polymer chains: 4
• Total formula weight: 108917.64

Authors

Cunningham Dueber, E.L.,Corn, J.E.,Bell, S.D.,Berger, J.M. (deposition date: 2007-06-18, release date: 2007-09-11, Last modification date: 2023-08-30)

Primary citation

Dueber, E.L.,Corn, J.E.,Bell, S.D.,Berger, J.M.
Replication origin recognition and deformation by a heterodimeric archaeal Orc1 complex.
Science, 317:1210-1213, 2007

PubMed 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.

PubMed: 17761879
DOI: 10.1126/science.1143690

Experimental method

X-RAY DIFFRACTION (3.35 Å)