A unified DNA- and dNTP-binding mode for DNA polymerases

Kamalendra Singh, Mukund J. Modak

Research output: Contribution to journalArticlepeer-review

22 Scopus citations

Abstract

Crystal structures of various DNA polymerases show a common structural topology that resembles a right hand and has distinct finger, palm and thumb subdomains. Early models of the Klenow fragment (KF) of Escherichia coli polymerase I showed DNA entering a large cleft that faces the palm subdomain where the catalytic site is situated. However, subsequent resolution of the structures of HIV-1 reverse transcriptase, KF and polymerase β (pol β) bound to DNA yielded conflicting data that suggested a different orientation for DNA bound to pol β compared with DNA bound to other polymerases. The debate, on the correct orientation of the template-primer DNA, that followed failed to reach a consensus. Using an alternative superposition scheme, we now provide convincing evidence for a common DNA-binding mode that is applicable to all polymerases, including pol β. Copyright (C) 1998 Elsevier Science Ltd.

Original languageEnglish (US)
Pages (from-to)277-281
Number of pages5
JournalTrends in Biochemical Sciences
Volume23
Issue number8
DOIs
StatePublished - Aug 1 1998

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

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