1FNN

CRYSTAL STRUCTURE OF CDC6P FROM PYROBACULUM AEROPHILUM

Summary for 1FNN

• Entry DOI: 10.2210/pdb1fnn/pdb
• Descriptor: CELL DIVISION CONTROL PROTEIN 6, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: cdc6, cdc18, orc1, aaa protein, dna replication initation factor, cell cycle control factor, cell cycle
• Biological source: Pyrobaculum aerophilum
• Total number of polymer chains: 2
• Total formula weight: 89428.64

Authors

Liu, J.,Smith, C.L.,DeRyckere, D.,DeAngelis, K.,Martin, G.S.,Berger, J.M. (deposition date: 2000-08-22, release date: 2000-10-04, Last modification date: 2024-02-07)

Primary citation

Liu, J.,Smith, C.L.,DeRyckere, D.,DeAngelis, K.,Martin, G.S.,Berger, J.M.
Structure and function of Cdc6/Cdc18: implications for origin recognition and checkpoint control.
Mol.Cell, 6:637-648, 2000

PubMed 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.

PubMed: 11030343
DOI: 10.1016/S1097-2765(00)00062-9

Experimental method

X-RAY DIFFRACTION (2 Å)