A closed conformation for the Pol lambda catalytic cycle.
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.
Garcia-Diaz
Miguel
M
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.
Bebenek
Katarzyna
K
Krahn
Joseph M
JM
Kunkel
Thomas A
TA
Pedersen
Lars C
LC
D002384:Catalysis; D018360:Crystallography, X-Ray; D019951:DNA Polymerase beta / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D011487:Protein Conformation
C415367:DNA polymerase beta2; D019951:DNA Polymerase beta