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Structure paper

TitleStructural basis for the phosphatase activity of polynucleotide kinase/phosphatase on single- and double-stranded DNA substrates.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 108, Page 21022-21027, Year 2011
Publish dateOct 13, 2011 (structure data deposition date)
AuthorsCoquelle, N. / Havali-Shahriari, Z. / Bernstein, N. / Green, R. / Glover, J.N.
External linksProc. Natl. Acad. Sci. USA / PubMed:22171004
MethodsX-ray diffraction
Resolution1.7 - 2.1 Å
Structure data

PDB-3u7e:
Crystal structure of mPNKP catalytic fragment (D170A)
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-3u7f:
Crystal structure of mPNKP catalytic fragment (D170A) bound to single-stranded DNA (TCCTCp)
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-3u7g:
Crystal structure of mPNKP catalytic fragment (D170A) bound to single-stranded DNA (TCCTAp)
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-3u7h:
Crystal structure of mPNKP catalytic fragment (D170A) bound to single-stranded DNA (TCCTTp)
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION

ChemComp-MG:
Unknown entry

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • mus musculus (house mouse)
KeywordsHYDROLASE / TRANSFERASE / protein-DNA complex / HAD family / pnkp / DNA repair / phosphatase / TRANSFERASE/DNA / TRANSFERASE-DNA complex

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