UvrABC

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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='' >
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== 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]].
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== Structural highlights ==
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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 07:43, 12 December 2016

UvrA complex with DNA, pyrophosphate and Zn+2 ion (grey) 3pih

Drag the structure with the mouse to rotate

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. 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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Michal Harel, Alexander Berchansky

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