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Structure paper

TitleThe ATPase mechanism of UvrA2 reveals the distinct roles of proximal and distal ATPase sites in nucleotide excision repair.
Journal, issue, pagesNucleic Acids Res., Vol. 47, Page 4136-4152, Year 2019
Publish dateDec 3, 2018 (structure data deposition date)
AuthorsCase, B.C. / Hartley, S. / Osuga, M. / Jeruzalmi, D. / Hingorani, M.M.
External linksNucleic Acids Res. / PubMed:30892613
MethodsX-ray diffraction
Resolution2.01 Å
Structure data

PDB-6n9l:
Crystal structure of T. maritima UvrA d117-399 with ADP
Method: X-RAY DIFFRACTION / Resolution: 2.01 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-HOH:
WATER

Source
  • thermotoga maritima (bacteria)
KeywordsDNA BINDING PROTEIN / UvrA / Nucleotide Excision Repair / NER / ADP / hydrolase / DNA damage repair

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