UvrABC

From Proteopedia

spinqualitylabelsall models UvrA complex with DNA, pyrophosphate and Zn+2 ion (grey) 3pih Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function UvrABC endonuclease is an E. coli enzyme complex involved in DNA repair. UvrABC removes 12 nucleotides around a DNA mutation replacing them with the correct one[1]. UvrA is the protein which locates the DNA damage. UvrB is involved in distinguishing damaged from undamaged DNA[2]. The C-terminal region of UvrC is involved in DNA binding and incisions at the 5'-side of a DNA damage during nucleotide excision repair[3]. UvrD is DNA helicase II. See Helicase. For details on the UvrA-UvrB complex see UvrA-UvrB interaction domains. Structural highlights UvrA contains several domains: UvrB-binding, DNA-binding and two ATP-binding domains[4].

3D structures of UvrABC

Updated on 12-December-2016

References

1. ↑ Moolenaar GF, Moorman C, Goosen N. Role of the Escherichia coli nucleotide excision repair proteins in DNA replication. J Bacteriol. 2000 Oct;182(20):5706-14. PMID:11004168
2. ↑ Theis K, Skorvaga M, Machius M, Nakagawa N, Van Houten B, Kisker C. The nucleotide excision repair protein UvrB, a helicase-like enzyme with a catch. Mutat Res. 2000 Aug 30;460(3-4):277-300. PMID:10946234
3. ↑ Moolenaar GF, Uiterkamp RS, Zwijnenburg DA, Goosen N. The C-terminal region of the Escherichia coli UvrC protein, which is homologous to the C-terminal region of the human ERCC1 protein, is involved in DNA binding and 5'-incision. Nucleic Acids Res. 1998 Jan 15;26(2):462-8. PMID:9421501
4. ↑ Jaciuk M, Nowak E, Skowronek K, Tanska A, Nowotny M. Structure of UvrA nucleotide excision repair protein in complex with modified DNA. Nat Struct Mol Biol. 2011 Feb;18(2):191-7. Epub 2011 Jan 16. PMID:21240268 doi:10.1038/nsmb.1973