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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 66 (Pt 9): 1013-8

PMID: 20823515 · PMCID: PMC2935216 · DOI:10.1107/S1744309110029374

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.

MeSH Terms (11)

Biocatalysis Calcium Catalytic Domain Cations, Divalent Crystallography, X-Ray DNA Polymerase beta Magnesium Models, Molecular Protein Binding Structural Homology, Protein Sulfolobus solfataricus

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