1v33
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Crystal structure of DNA primase from Pyrococcus horikoshii
OverviewOverview
BACKGROUND: In chromosomal DNA replication, DNA primase initiates the, synthesis of a dinucleotide on a single-stranded template DNA, and, elongates it to form a primer RNA for the replicative DNA polymerase., Although the apo-structure of an archaeal primase has been reported, the, mechanism of primer synthesis by the eukaryotic-type primase still remains, to be elucidated. RESULTS: In this study, we present the crystal structure, of the eukaryotic-type DNA primase from the hyperthermophilic archaeon, (Pyrococcus horikoshii) with the uridine 5'-triphosphate (UTP). In the, present primase-UTP complex, the primase binds the triphosphate moiety of, the UTP at the active site, which includes Asp95, Asp97, and Asp280, the, essential residues for the nucleotidyl transfer reaction. CONCLUSION: The, nucleotide binding geometry in this complex explains the previous, biochemical analyses of the eukaryotic primase. Based on the complex, structure, we constructed a model between the DNA primase and a, primer/template DNA for the primer synthesis. This model facilitates the, comprehension of the reported features of DNA primase.
About this StructureAbout this Structure
1V33 is a Single protein structure of sequence from Pyrococcus horikoshii with ZN and PO4 as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the Pyrococcus horikoshii DNA primase-UTP complex: implications for the mechanism of primer synthesis., Ito N, Nureki O, Shirouzu M, Yokoyama S, Hanaoka F, Genes Cells. 2003 Dec;8(12):913-23. PMID:14750947
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