1ZT2
Heterodimeric structure of the core primase.
Summary for 1ZT2
| Entry DOI | 10.2210/pdb1zt2/pdb |
| Descriptor | DNA primase small subunit, DNA primase large subunit, ZINC ION, ... (5 entities in total) |
| Functional Keywords | heterodimeric complex, replication, transferase |
| Biological source | Sulfolobus solfataricus More |
| Total number of polymer chains | 4 |
| Total formula weight | 128977.56 |
| Authors | Lao-Sirieix, S.H.,Nookala, R.K.,Roversi, P.,Bell, S.D.,Pellegrini, L. (deposition date: 2005-05-26, release date: 2005-11-08, Last modification date: 2024-11-20) |
| Primary citation | Lao-Sirieix, S.H.,Nookala, R.K.,Roversi, P.,Bell, S.D.,Pellegrini, L. Structure of the heterodimeric core primase. Nat.Struct.Mol.Biol., 12:1137-1144, 2005 Cited by PubMed Abstract: 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. PubMed: 16273105DOI: 10.1038/nsmb1013 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.33 Å) |
Structure validation
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