Crystallization and preliminary X-ray diffraction analysis of motif N from Saccharomyces cerevisiae Dbf4.
The Cdc7-Dbf4 complex plays an instrumental role in the initiation of DNA replication and is a target of replication-checkpoint responses in Saccharomyces cerevisiae. Cdc7 is a conserved serine/threonine kinase whose activity depends on association with its regulatory subunit, Dbf4. A conserved sequence near the N-terminus of Dbf4 (motif N) is necessary for the interaction of Cdc7-Dbf4 with the checkpoint kinase Rad53. To understand the role of the Cdc7-Dbf4 complex in checkpoint responses, a fragment of Saccharomyces cerevisiae Dbf4 encompassing motif N was isolated, overproduced and crystallized. A complete native data set was collected at 100 K from crystals that diffracted X-rays to 2.75 A resolution and structure determination is currently under way.
Matthews
Lindsay A
LA
Department of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, ON, Canada.
Duong
Andrew
A
Prasad
Ajai A
AA
Duncker
Bernard P
BP
Guarné
Alba
A
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D018797:Cell Cycle Proteins / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D012441:Saccharomyces cerevisiae / Q000737:chemistry*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000302:isolation & purification; D014961:X-Ray Diffraction
D018797:Cell Cycle Proteins; C088096:Dbf4 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins