UvrABC: Difference between revisions

Revision as of 15:22, 10 October 2019

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^[2].
UvrB is involved in distinguishing damaged from undamaged DNA^[3].
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^[4].
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: ^[5].

3D structures of UvrABC3D structures of UvrABC

Updated on 10-October-2019

ReferencesReferences

↑ 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
↑ 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
↑ 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
↑ 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
↑ 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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

[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] 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

[3] 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

[4] 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

[5] 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

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 == Structural highlights ==
-UvrA contains several domains: <scene name='53/536710/Cv/1'>UvrB-binding, DNA-binding and two ATP-binding domains</scene><ref>PMID:21240268</ref>.
+UvrA contains several domains: <scene name='53/536710/Cv/2'>UvrB-binding, DNA-binding and two ATP-binding domains</scene><ref>PMID:21240268</ref>.
 </StructureSection>
 ==3D structures of UvrABC==