5DMP

Structure of the Archaeal NHEJ Phosphoesterase from Methanocella paludicola.

5DMP の概要

• エントリーDOI: 10.2210/pdb5dmp/pdb
• 分子名称: Uncharacterized protein, 1,2-ETHANEDIOL, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: archaeal proteins, biocatalysis, dna repair enzymes, phosphoric diester hydrolases, phosphoric monoester hydrolases, hydrolase
• 由来する生物種: Methanocella paludicola
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19620.51

構造登録者

Brissett, N.C.,Bartlett, E.J.,Doherty, A.J. (登録日: 2015-09-09, 公開日: 2015-10-07, 最終更新日: 2024-01-10)

主引用文献

Bartlett, E.J.,Brissett, N.C.,Plocinski, P.,Carlberg, T.,Doherty, A.J.
Molecular basis for DNA strand displacement by NHEJ repair polymerases.
Nucleic Acids Res., 44:2173-2186, 2016

PubMed Abstract: The non-homologous end-joining (NHEJ) pathway repairs DNA double-strand breaks (DSBs) in all domains of life. Archaea and bacteria utilize a conserved set of multifunctional proteins in a pathway termed Archaeo-Prokaryotic (AP) NHEJ that facilitates DSB repair. Archaeal NHEJ polymerases (Pol) are capable of strand displacement synthesis, whilst filling DNA gaps or partially annealed DNA ends, which can give rise to unligatable intermediates. However, an associated NHEJ phosphoesterase (PE) resects these products to ensure that efficient ligation occurs. Here, we describe the crystal structures of these archaeal (Methanocella paludicola) NHEJ nuclease and polymerase enzymes, demonstrating their strict structural conservation with their bacterial NHEJ counterparts. Structural analysis, in conjunction with biochemical studies, has uncovered the molecular basis for DNA strand displacement synthesis in AP-NHEJ, revealing the mechanisms that enable Pol and PE to displace annealed bases to facilitate their respective roles in DSB repair.

PubMed: 26405198
DOI: 10.1093/nar/gkv965

実験手法

X-RAY DIFFRACTION (1.793 Å)