1zt2 | pdb_00001zt2
Heterodimeric structure of the core primase.
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| 1zt2, resolution 3.33Å | |||||||||||||
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| Ligands: | SO4, ZN | ||||||||||||
| Gene: | priA (Sulfolobus solfataricus), priB (Sulfolobus solfataricus) | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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
Page seeded by OCA on Mon Mar 31 01:41:16 2008
