A closed conformation for the Pol λ catalytic cycle
- 19 December 2004
- journal article
- research article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 12 (1) , 97-98
- https://doi.org/10.1038/nsmb876
Abstract
Pol λ is a family X member believed to fill short gaps during DNA repair. Here we report crystal structures of Pol λ representing three steps in filling a single-nucleotide gap. These structures indicate that, unlike other DNA polymerases, Pol λ 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.Keywords
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