| Literature DB >> 11030343 |
J Liu1, C L Smith, D DeRyckere, K DeAngelis, G S Martin, J M Berger.
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.Entities:
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Year: 2000 PMID: 11030343 DOI: 10.1016/s1097-2765(00)00062-9
Source DB: PubMed Journal: Mol Cell ISSN: 1097-2765 Impact factor: 17.970