Metal-ion dependence of the active-site conformation of the translesion DNA polymerase Dpo4 from Sulfolobus solfataricus.

Irimia A, Loukachevitch LV, Eoff RL, Guengerich FP, Egli M
Acta Crystallogr Sect F Struct Biol Cryst Commun (2010), Volume 66, Page 1013
PubMed entry Full article text Publisher's site

Abstract:

Crystal structures of a binary Mg2+-form Dpo4-DNA complex with ...
Crystal structures of a binary Mg2+-form Dpo4-DNA complex with 1,N2-etheno-dG in the template strand as well as of ternary Mg2+-form Dpo4-DNA-dCTP/dGTP complexes with 8-oxoG in the template strand have been determined. Comparison of their conformations and active-site geometries with those of the corresponding Ca2+-form complexes revealed that the DNA and polymerase undergo subtle changes as a result of the catalytically more active Mg2+ occupying both the A and B sites.

Polymerases:

Dpo4

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