title: A closed conformation for the Pol lambda catalytic cycle.
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.
authors.affiliation: Laboratory of Structural Biology, National Institute of Environmental Health Sciences, National Institutes of Health, Department of Health and Human Services, Research Triangle Park, North Carolina 27709, USA.
authors.forename: Miguel
authors.initials: M
authors.lastname: Garcia-Diaz
authors.forename: Katarzyna
authors.initials: K
authors.lastname: Bebenek
authors.forename: Joseph M
authors.initials: JM
authors.lastname: Krahn
authors.forename: Thomas A
authors.initials: TA
authors.lastname: Kunkel
authors.forename: Lars C
authors.initials: LC
authors.lastname: Pedersen
mesh_terms: D002384:Catalysis; D018360:Crystallography, X-Ray; D019951:DNA Polymerase beta / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D011487:Protein Conformation
chemical_list: C415367:DNA polymerase beta2; D019951:DNA Polymerase beta