A closed conformation for the Pol lambda catalytic cycle

Pollambda is a family X member believed to fill short gaps during DNA repair. Here we report crystal structures of Pollambda representing three steps in filling a single-nucleotide gap. These structures indicate that, unlike other DNA polymerases, Pollambda 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.