1zt2

From Proteopedia

Revision as of 05:31, 21 November 2007

Heterodimeric structure of the core primase.

Overview

Primases are DNA-dependent RNA polymerases that synthesize the, oligoribonucleotide primers essential to DNA replication. In archaeal and, eukaryotic organisms, the core primase is a heterodimeric enzyme composed, of a small and a large subunit. Here we report a crystallographic and, biochemical analysis of the core primase from the archaeon Sulfolobus, solfataricus. The structure provides the first three-dimensional, description of the large subunit and its interaction with the small, subunit. The evolutionary conservation of amino acids at the, protein-protein interface implies that the observed mode of subunit, association is conserved among archaeal and eukaryotic primases. The, orientation of the large subunit in the core primase probably excludes its, direct involvement in catalysis. Modeling of a DNA-RNA helix together with, structure-based site-directed mutagenesis provides insight into the, mechanism of template DNA binding and RNA primer synthesis.

About this Structure

1ZT2 is a Protein complex structure of sequences from Sulfolobus solfataricus with ZN and SO4 as ligands. Full crystallographic information is available from OCA.

Reference

Structure of the heterodimeric core primase., Lao-Sirieix SH, Nookala RK, Roversi P, Bell SD, Pellegrini L, Nat Struct Mol Biol. 2005 Dec;12(12):1137-44. Epub 2005 Nov 6. PMID:16273105

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