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| <StructureSection load='3pih' size='340' side='right' caption='UvrA complex with DNA, pyrophosphate and Zn+2 ion (grey) [[3pih]]' scene='' > | | <StructureSection load='3pih' size='340' side='right' caption='UvrA complex with DNA, pyrophosphate and Zn+2 ion (grey) [[3pih]]' scene='53/536710/Cv/3' > |
| == Function == | | == 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<ref>PMID:11004168</ref>.<br /> | | '''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<ref>PMID:11004168</ref>.<br /> |
Revision as of 12:06, 13 January 2022
| 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: UvrB-binding, DNA-binding and two ATP-binding domains[5].
- ↑ 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
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3D structures of UvrABC
Updated on 13-January-2022
{"openlevels":0}
- UvrA
- Helicase – TmUvrA + DNA – Thermotoga maritima
- UvrA-UvrB interaction domains - TmUvrA (mutant) + ADP
- 3zqj – UvrA – Mycobacterium tuberculosis
- 4dfc – EcUvrA + Transcription-repair-coupling factor – Escherichia coli
- 2r6f – BstUvrA – Bacillus stearothermophilus
- 3ux8 – GeUvrA - Geobacillus
- 2vf7, 2vf8 – DrUvrA2 - Deinococcus radiodurans
- UvrB
- UvrC
- 1kft, 1qoj – EcUvrC C terminal
- 1e52 – EcUvrC C terminal - NMR
- 2nrr, 2nrt, 2nrv, 2nrw, 2nrx, 2nrz – TmUvrC C terminal
- 1ycz, 1yd0, 1yd1 – TmUvrC N terminal
- 1yd2, 1yd3, 1yd4, 1yd5 – TmUvrC N terminal (mutant)
- 1yd6 – BcUvrC N terminal
- 3c65 – BstUvrC
- UvrD or DNA helicase II see Helicase
- UvrA-UvrB
- 3fpn – BstUvrA + UvrB
- 3uwx – GeUvrA + UvrB
References
