5OFN

Crystal structure of the heterotrimeric PriSLX primase from S. solfataricus.

5OFN の概要

• エントリーDOI: 10.2210/pdb5ofn/pdb
• 分子名称: DNA primase small subunit PriS, DNA primase large subunit PriL,PriL-X fusion protein, ZINC ION, ... (4 entities in total)
• 機能のキーワード: primase, dna-dependent rna polymerase, dna replication, replication
• 由来する生物種: Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 114056.58

構造登録者

Pellegrini, L.,Holzer, S. (登録日: 2017-07-11, 公開日: 2017-11-29, 最終更新日: 2024-01-17)

主引用文献

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

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: 29167441
DOI: 10.1038/s41467-017-01707-w

実験手法

X-RAY DIFFRACTION (3.005 Å)