7OLA

Structure of Primase-Helicase in SaPI5

7OLA の概要

• エントリーDOI: 10.2210/pdb7ola/pdb
• EMDBエントリー: 12975
• 分子名称: DNA primase, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: helicase, dna binding, amppnp, replication
• 由来する生物種: Staphylococcus aureus
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 560139.89

構造登録者

Qiao, C.C.,Mir-Sanchis, I. (登録日: 2021-05-19, 公開日: 2022-07-13, 最終更新日: 2024-11-13)

主引用文献

Qiao, C.,Debiasi-Anders, G.,Mir-Sanchis, I.
Staphylococcal self-loading helicases couple the staircase mechanism with inter domain high flexibility.
Nucleic Acids Res., 50:8349-8362, 2022

PubMed Abstract: Replication is a crucial cellular process. Replicative helicases unwind DNA providing the template strand to the polymerase and promoting replication fork progression. Helicases are multi-domain proteins which use an ATPase domain to couple ATP hydrolysis with translocation, however the role that the other domains might have during translocation remains elusive. Here, we studied the unexplored self-loading helicases called Reps, present in Staphylococcus aureus pathogenicity islands (SaPIs). Our cryoEM structures of the PriRep5 from SaPI5 (3.3 Å), the Rep1 from SaPI1 (3.9 Å) and Rep1-DNA complex (3.1Å) showed that in both Reps, the C-terminal domain (CTD) undergoes two distinct movements respect the ATPase domain. We experimentally demonstrate both in vitro and in vivo that SaPI-encoded Reps need key amino acids involved in the staircase mechanism of translocation. Additionally, we demonstrate that the CTD's presence is necessary for the maintenance of full ATPase and helicase activities. We speculate that this high interdomain flexibility couples Rep's activities as initiators and as helicases.

PubMed: 35871290
DOI: 10.1093/nar/gkac625

実験手法

ELECTRON MICROSCOPY (3.3 Å)