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Structure paper

TitleStructure of the C-terminal half of UvrC reveals an RNase H endonuclease domain with an Argonaute-like catalytic triad.
Journal, issue, pagesEmbo J., Vol. 26, Page 613-622, Year 2007
Publish dateNov 2, 2006 (structure data deposition date)
AuthorsKarakas, E. / Truglio, J.J. / Croteau, D. / Rhau, B. / Wang, L. / Van Houten, B. / Kisker, C.
External linksEmbo J. / PubMed:17245438
MethodsX-ray diffraction
Resolution1.2 - 2.3 Å
Structure data

PDB-2nrr:
Crystal structure of the C-terminal RNAseH endonuclase domain of UvrC
Method: X-RAY DIFFRACTION / Resolution: 1.2 Å

PDB-2nrt:
Crystal structure of the C-terminal half of UvrC
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-2nrv:
Crystal structure of the C-terminal half of UvrC
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-2nrw:
Crystal structure of the C terminal half of UvrC
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-2nrx:
Crystal structure of the C-terminal half of UvrC, in the presence of sulfate molecules
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-2nrz:
Crystal structure of the C-terminal half of UvrC bound to its catalytic divalent cation
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-CL:
Unknown entry

ChemComp-NA:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-MN:
Unknown entry

Source
  • thermotoga maritima (bacteria)
KeywordsHYDROLASE / UvrC / endonuclase / NER / endonuclease / RNAse H / helix hairpin helix / UvrABC / divalent cation / manganese

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