5DMP

Structure of the Archaeal NHEJ Phosphoesterase from Methanocella paludicola.

Summary for 5DMP

• Entry DOI: 10.2210/pdb5dmp/pdb
• Descriptor: Uncharacterized protein, 1,2-ETHANEDIOL, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: archaeal proteins, biocatalysis, dna repair enzymes, phosphoric diester hydrolases, phosphoric monoester hydrolases, hydrolase
• Biological source: Methanocella paludicola
• Total number of polymer chains: 1
• Total formula weight: 19620.51

Authors

Brissett, N.C.,Bartlett, E.J.,Doherty, A.J. (deposition date: 2015-09-09, release date: 2015-10-07, Last modification date: 2024-01-10)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.793 Å)