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.
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Acknowledgements
The authors thank W. Beard, L. Pedersen and J. Boyington for critical review of the manuscript. Use of the Advanced Photon Source was supported by the US Department of Energy, Office of Science, Office of Basic Energy Sciences, under contract no. W-31-109-Eng-38.
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Supplementary information
Supplementary Fig. 1
Superimposition of Pol γ complexes (PDF 221 kb)
Supplementary Fig. 2
Minor groove interactions in the active site. (PDF 81 kb)
Supplementary Fig. 3
Coordination of the ddTTP with the catalytic metal. (PDF 125 kb)
Supplementary Table 1
Crystallographic data statistics. (PDF 55 kb)
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Garcia-Diaz, M., Bebenek, K., Krahn, J. et al. A closed conformation for the Pol λ catalytic cycle. Nat Struct Mol Biol 12, 97–98 (2005). https://doi.org/10.1038/nsmb876
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DOI: https://doi.org/10.1038/nsmb876
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