1fnn
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(New page: 200px<br /><applet load="1fnn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fnn, resolution 2.0Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 21:59, 24 November 2007
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CRYSTAL STRUCTURE OF CDC6P FROM PYROBACULUM AEROPHILUM
Overview
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.
About this Structure
1FNN is a Single protein structure of sequence from Pyrobaculum aerophilum with MG and ADP as ligands. Full crystallographic information is available from OCA.
Reference
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
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