Structural highlights
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
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.
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 Mol Cell. 2000 Sep;6(3):637-48. PMID:11030343[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Liu J, Smith CL, DeRyckere D, DeAngelis K, Martin GS, Berger JM. Structure and function of Cdc6/Cdc18: implications for origin recognition and checkpoint control. Mol Cell. 2000 Sep;6(3):637-48. PMID:11030343
