5dmp | pdb_00005dmp

Structure of the Archaeal NHEJ Phosphoesterase from Methanocella paludicola.

spinqualitylabelsall models 5dmp, resolution 1.79Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5dmp is a 1 chain structure with sequence from Methanocella paludicola. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.793Å Ligands: EDO, MG, VN4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D1Z0H7_METPS Publication Abstract from PubMed 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. Molecular basis for DNA strand displacement by NHEJ repair polymerases.,Bartlett EJ, Brissett NC, Plocinski P, Carlberg T, Doherty AJ Nucleic Acids Res. 2015 Sep 23. pii: gkv965. PMID:26405198 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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