Mol Cell. 2000 Sep;6(3):637-48.

Structure and function of Cdc6/Cdc18: implications for origin recognition and checkpoint control.

Liu J, Smith CL, DeRyckere D, DeAngelis K, Martin GS, Berger JM.

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Department of Molecular and Cell Biology, University of California, Berkeley 94720, USA.

Abstract

Cdc6/Cdc18 is a conserved and essential component of prereplication complexes. The 2.0 A crystal structure of an archaeal Cdc6 ortholog, in conjunction with a mutational analysis of the homologous Cdc18 protein from Schizosaccharomyces pombe, reveals novel aspects of Cdc6/Cdc18 function. Two domains of Cdc6 form an AAA+-type nucleotide binding fold that is observed bound to Mg.ADP. A third domain adopts a winged-helix fold similar to known DNA binding modules. Sequence comparisons show that the winged-helix domain is conserved in Orc1, and mutagenesis data demonstrate that this region of Cdc6/Cdc18 is required for function in vivo. Additional mutational analyses suggest that nucleotide binding and/or hydrolysis by Cdc6/Cdc18 is required not only for progression through S phase, but also for maintenance of checkpoint control during S phase.

PMID:: 11030343; [PubMed - indexed for MEDLINE]

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Structures reported by this article

Crystal Structure Of Cdc6p From Pyrobaculum Aerophilum

PDB: 1FNN

Source: Pyrobaculum aerophilum

Method: X-Ray Diffraction

Resolution: 2 Å

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