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Crystallization and preliminary X-ray diffraction analysis of motif N from Saccharomyces cerevisiae Dbf4.

ABSTRACT: 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.

SUBMITTER: Matthews LA

PROVIDER: S-EPMC2795593 | biostudies-literature | 2009 Sep

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray diffraction analysis of motif N from Saccharomyces cerevisiae Dbf4.

Matthews Lindsay A LA Duong Andrew A Prasad Ajai A AA Duncker Bernard P BP Guarné Alba A

Acta crystallographica. Section F, Structural biology and crystallization communications 20090822 Pt 9

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 fr ...[more]

PMID: 19724125

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