2QBY

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

2QBY の概要

• エントリーDOI: 10.2210/pdb2qby/pdb
• 分子名称: DNA (33-MER), Cell division control protein 6 homolog 1, Cell division control protein 6 homolog 3, ... (9 entities in total)
• 機能のキーワード: winged-helix domain, helix-turn-helix, aaa+ atpase domain, protein-dna complex, double helix, replication-dna complex, replication/dna
• 由来する生物種: Sulfolobus solfataricus; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 108917.64

構造登録者

Cunningham Dueber, E.L.,Corn, J.E.,Bell, S.D.,Berger, J.M. (登録日: 2007-06-18, 公開日: 2007-09-11, 最終更新日: 2023-08-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.35 Å)