A closed conformation for the Pol lambda catalytic cycle

Nat Struct Mol Biol. 2005 Jan;12(1):97-8. doi: 10.1038/nsmb876. Epub 2004 Dec 19.

Abstract

Pol lambda is a family X member believed to fill short gaps during DNA repair. Here we report crystal structures of Pol lambda representing three steps in filling a single-nucleotide gap. These structures indicate that, unlike other DNA polymerases, Pol lambda does not undergo large subdomain movements during catalysis, and they provide a clear characterization of the geometry and stereochemistry of the in-line nucleotidyl transfer reaction.

Publication types

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

MeSH terms

  • Catalysis
  • Crystallography, X-Ray
  • DNA Polymerase beta / chemistry*
  • DNA Polymerase beta / metabolism*
  • Humans
  • Models, Molecular
  • Protein Conformation

Substances

  • DNA polymerase beta2
  • DNA Polymerase beta

Associated data

  • PDB/1XSL
  • PDB/1XSN
  • PDB/1XSP