5op0

Structure of Prim-PolC from Mycobacterium smegmatis

spinqualitylabelsall models 5op0, resolution 1.84Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5op0 is a 2 chain structure with sequence from Mycolicibacterium smegmatis MC2 155. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.84Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0R5T1_MYCS2 Publication Abstract from PubMed 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. DNA Ligase C and Prim-PolC participate in base excision repair in mycobacteria.,Plocinski P, Brissett NC, Bianchi J, Brzostek A, Korycka-Machala M, Dziembowski A, Dziadek J, Doherty AJ Nat Commun. 2017 Nov 1;8(1):1251. doi: 10.1038/s41467-017-01365-y. PMID:29089537 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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