5OP0

Structure of Prim-PolC from Mycobacterium smegmatis

5OP0 の概要

• エントリーDOI: 10.2210/pdb5op0/pdb
• 分子名称: DNA polymerase LigD, polymerase domain (2 entities in total)
• 機能のキーワード: nucleotidyl transferase, polymerase, base excision repair, transferase
• 由来する生物種: Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 74428.16

構造登録者

Brissett, N.C.,Doherty, A.J. (登録日: 2017-08-09, 公開日: 2017-11-15, 最終更新日: 2024-11-13)

主引用文献

Pocinski, P.,Brissett, N.C.,Bianchi, J.,Brzostek, A.,Korycka-Machaa, M.,Dziembowski, A.,Dziadek, J.,Doherty, A.J.
DNA Ligase C and Prim-PolC participate in base excision repair in mycobacteria.
Nat Commun, 8:1251-1251, 2017

PubMed Abstract: Prokaryotic Ligase D is a conserved DNA repair apparatus processing DNA double-strand breaks in stationary phase. An orthologous Ligase C (LigC) complex also co-exists in many bacterial species but its function is unknown. Here we show that the LigC complex interacts with core BER enzymes in vivo and demonstrate that together these factors constitute an excision repair apparatus capable of repairing damaged bases and abasic sites. The polymerase component, which contains a conserved C-terminal structural loop, preferentially binds to and fills-in short gapped DNA intermediates with RNA and LigC ligates the resulting nicks to complete repair. Components of the LigC complex, like LigD, are expressed upon entry into stationary phase and cells lacking either of these pathways exhibit increased sensitivity to oxidising genotoxins. Together, these findings establish that the LigC complex is directly involved in an excision repair pathway(s) that repairs DNA damage with ribonucleotides during stationary phase.

PubMed: 29089537
DOI: 10.1038/s41467-017-01365-y

実験手法

X-RAY DIFFRACTION (1.84 Å)