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

A closed conformation for the Pol lambda catalytic cycle

Miguel Garcia-Diaz  1 , Katarzyna Bebenek, Joseph M Krahn, Thomas A Kunkel, Lars C Pedersen
Affiliations

A closed conformation for the Pol lambda catalytic cycle

Miguel Garcia-Diaz et al. Nat Struct Mol Biol. 2005 Jan.

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.

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