2qby

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

spinqualitylabelsall models 2qby, resolution 3.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2qby is a 4 chain structure with sequence from Saccharolobus solfataricus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.35Å Ligands: ADP, K, MG, SPD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CDC61_SACS2 Involved in regulation of DNA replication. May play essential roles in origin recognition and cell cycle control of replication. Binds to DNA, with a preference for molecules that contain a bubble, a fork, or a tail. Inhibits the binding of the MCM helicase to the origin DNA and strongly inhibits its DNA helicase activity. Also regulates the DNA polymerase and the nuclease activities of PolB1. Stimulates the DNA-binding activity of Cdc6-3.[HAMAP-Rule:MF_01407] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Replication origin recognition and deformation by a heterodimeric archaeal Orc1 complex.,Dueber EL, Corn JE, Bell SD, Berger JM Science. 2007 Aug 31;317(5842):1210-3. PMID:17761879 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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