Structure and mechanism of DNA polymerases

Adv Protein Chem. 2005;71:401-40. doi: 10.1016/S0065-3233(04)71011-6.

Abstract

DNA polymerases are molecular motors directing the synthesis of DNA from nucleotides. All polymerases have a common architectural framework consisting of three canonical subdomains termed the fingers, palm, and thumb subdomains. Kinetically, they cycle through various states corresponding to conformational transitions, which may or may not generate force. In this review, we present and discuss the kinetic, structural, and single-molecule works that have contributed to our understanding of DNA polymerase function.

Publication types

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

MeSH terms

  • Animals
  • Catalysis
  • DNA / chemistry
  • DNA / physiology
  • DNA-Directed DNA Polymerase / chemistry*
  • DNA-Directed DNA Polymerase / physiology*
  • Humans
  • Nucleotides / chemistry
  • Nucleotides / physiology
  • Protein Conformation
  • Protein Structure, Tertiary

Substances

  • Nucleotides
  • DNA
  • DNA-Directed DNA Polymerase