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

Laura F. Silvian, Eric A. Toth, Phuong Pham, Myron F. Goodman, Tom Ellenberger

Research output: Contribution to journalArticle

147 Scopus citations

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 Å resolution crystal structure of the Sulfolobus solfataricus Dbh protein, a DNA translesion polymerase closely related to Escherichia coli DNA polymerase IV and human polymerase κ. 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.

Original languageEnglish
Pages (from-to)984-989
Number of pages6
JournalNature Structural Biology
Volume8
Issue number11
DOIs
StatePublished - Nov 15 2001

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    Silvian, L. F., Toth, E. A., Pham, P., Goodman, M. F., & Ellenberger, T. (2001). Crystal structure of a DinB family error-prone DNA polymerase from Sulfolobus solfataricus. Nature Structural Biology, 8(11), 984-989. https://doi.org/10.1038/nsb1101-984