Crystal structure of a DinB family error-prone DNA polymerase from Sulfolobus solfataricus

Nat Struct Biol. 2001 Nov;8(11):984-9. doi: 10.1038/nsb1101-984.


A new group of error-prone DNA polymerases overcomes the blockage posed to normal DNA replication by damaged template bases, suggesting an active site with a loose, flexible pocket that accommodates aberrant DNA structures. We have determined a 2.8 A resolution crystal structure of the Sulfolobus solfataricus Dbh protein, a DNA translesion polymerase closely related to Escherichia coli DNA polymerase IV and human polymerase kappa. A high error rate is observed for the Dbh polymerase in a range of 10(-2)-10(-3) for all 12 base substitution mispairs. The crystal structure of Dbh reveals an overall architecture resembling other DNA polymerases but has unique features that are likely to contribute to error-prone synthesis, including -1 frameshifting mutations.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Archaeal Proteins*
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism*
  • Catalysis
  • Conserved Sequence
  • Crystallography, X-Ray
  • DNA Polymerase beta / chemistry*
  • DNA-Directed DNA Polymerase*
  • Escherichia coli Proteins*
  • Humans
  • Kinetics
  • Models, Molecular
  • Molecular Sequence Data
  • Mutagenesis*
  • Protein Structure, Tertiary
  • Proteins / chemistry
  • Sequence Alignment
  • Sequence Homology, Amino Acid*
  • Sulfolobus / enzymology*
  • Taq Polymerase / metabolism


  • Archaeal Proteins
  • Bacterial Proteins
  • DinB protein, E coli
  • Escherichia coli Proteins
  • Proteins
  • Dbh protein, Sulfolobus solfataricus
  • Taq Polymerase
  • DNA Polymerase beta
  • DNA-Directed DNA Polymerase
  • POLK protein, human

Associated data

  • PDB/1K1Q
  • PDB/1K1S