Metal-ion dependence of the active-site conformation of the translesion DNA polymerase Dpo4 from Sulfolobus solfataricus

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Sep 1;66(Pt 9):1013-8. doi: 10.1107/S1744309110029374. Epub 2010 Aug 21.


Crystal structures of a binary Mg2+-form Dpo4-DNA complex with 1,N2-etheno-dG in the template strand as well as of ternary Mg2+-form Dpo4-DNA-dCTP/dGTP complexes with 8-oxoG in the template strand have been determined. Comparison of their conformations and active-site geometries with those of the corresponding Ca2+-form complexes revealed that the DNA and polymerase undergo subtle changes as a result of the catalytically more active Mg2+ occupying both the A and B sites.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Biocatalysis
  • Calcium / chemistry*
  • Calcium / metabolism
  • Catalytic Domain*
  • Cations, Divalent / chemistry
  • Cations, Divalent / metabolism
  • Crystallography, X-Ray
  • DNA Polymerase beta / chemistry*
  • Magnesium / chemistry*
  • Magnesium / metabolism
  • Models, Molecular
  • Protein Binding
  • Structural Homology, Protein
  • Sulfolobus solfataricus / enzymology*


  • Cations, Divalent
  • DNA Polymerase beta
  • Magnesium
  • Calcium

Associated data

  • PDB/2XC9
  • PDB/2XCA
  • PDB/2XCP