1ZT2: Heterodimeric Structure Of The Core Primase

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.
PDB ID: 1ZT2Download
MMDB ID: 36046
PDB Deposition Date: 2005/5/26
Updated in MMDB: 2005/12
Experimental Method:
x-ray diffraction
Resolution: 3.33  Å
Source Organism:
Similar Structures:
Biological Unit for 1ZT2: dimeric; determined by author and by software (PISA)
Molecular Components in 1ZT2
Label Count Molecule
Proteins (2 molecules)
DNA Primase Small Subunit(Gene symbol: SSO_RS05190)
Molecule annotation
DNA Primase Large Subunit(Gene symbol: SSO_RS02840)
Molecule annotation
Chemicals (24 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB