5OF3
Crystal structure of the heterotrimeric PriSLX primase from S. solfataricus.
Summary for 5OF3
| Entry DOI | 10.2210/pdb5of3/pdb |
| Descriptor | DNA primase small subunit PriS, DNA primase large subunit PriL, Uncharacterized protein, ... (6 entities in total) |
| Functional Keywords | primase, dna-dependent rna polymerase, dna replication, replication |
| Biological source | Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) More |
| Total number of polymer chains | 6 |
| Total formula weight | 185350.59 |
| Authors | Pellegrini, L.,Holzer, S. (deposition date: 2017-07-10, release date: 2017-11-29, Last modification date: 2024-11-20) |
| Primary citation | Holzer, S.,Yan, J.,Kilkenny, M.L.,Bell, S.D.,Pellegrini, L. Primer synthesis by a eukaryotic-like archaeal primase is independent of its Fe-S cluster. Nat Commun, 8:1718-1718, 2017 Cited by PubMed Abstract: DNA replication depends on primase, the specialised polymerase responsible for synthesis of the RNA primers that are elongated by the replicative DNA polymerases. In eukaryotic and archaeal replication, primase is a heterodimer of two subunits, PriS and PriL. Recently, a third primase subunit named PriX was identified in the archaeon Sulfolobus solfataricus. PriX is essential for primer synthesis and is structurally related to the Fe-S cluster domain of eukaryotic PriL. Here we show that PriX contains a nucleotide-binding site required for primer synthesis, and demonstrate equivalence of nucleotide-binding residues in PriX with eukaryotic PriL residues that are known to be important for primer synthesis. A primase chimera, where PriX is fused to a truncated version of PriL lacking the Fe-S cluster domain retains wild-type levels of primer synthesis. Our evidence shows that PriX has replaced PriL as the subunit that endows primase with the unique ability to initiate nucleic acid synthesis. Importantly, our findings reveal that the Fe-S cluster is not required for primer synthesis. PubMed: 29167441DOI: 10.1038/s41467-017-01707-w PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.906 Å) |
Structure validation
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