UvrABC: Difference between revisions
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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='' > | ||
== 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>. For details on the UvrA-UvrB complex see [[UvrA-UvrB interaction domains]]. | '''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>. 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<ref>PMID:21240268</ref>. | |||
</StructureSection> | </StructureSection> | ||
==3D structures of UvrABC== | ==3D structures of UvrABC== | ||
Revision as of 10:43, 12 December 2016
FunctionUvrABC 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]. For details on the UvrA-UvrB complex see UvrA-UvrB interaction domains. Structural highlightsUvrA contains several domains: UvrB-binding, DNA-binding and two ATP-binding domains[2]. |
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3D structures of UvrABC3D structures of UvrABC
Updated on 12-December-2016
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