Download MendeleyCrystal structure of a DinB family error-prone DNA polymerase from Sulfolobus solfataricus.
Silvian, L.F., Toth, E.A., Pham, P., Goodman, M.F., Ellenberger, T.(2001) Nat Struct Biol 8: 984-989
- PubMed: 11685247
- DOI: https://doi.org/10.1038/nsb1101-984
- Primary Citation of Related Structures:
1K1Q, 1K1S - PubMed Abstract:
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.
Organizational Affiliation:
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA.
