Structural and functional insights provided by crystal structures of DNA polymerases and their substrate complexes

Chad A Brautigam, Thomas A. Steitz

Research output: Contribution to journalArticle

307 Scopus citations

Abstract

New levels in the understanding of DNA replication have been achieved from recent crystal structure determinations of several DNA polymerases and their substrate complexes. The structure of an α family DNA polymerase from bacteriophage RB69 shows some similarities, but also considerable differences in structure and organization from the pol I family DNA polymerases. Also, the functions of three polymerase domains and their conserved residues have been clarified by studying structures of pol I family DNA polymerases complexed to their substrates. These structures also confirm that an identical two-metal ion catalytic mechanism proposed previously is used by both the nonhomologous pol I and pol β family DNA polymerases.

Original languageEnglish (US)
Pages (from-to)54-63
Number of pages10
JournalCurrent Opinion in Structural Biology
Volume8
Issue number1
DOIs
StatePublished - Feb 1998

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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