title: Metal-ion dependence of the active-site conformation of the translesion DNA polymerase Dpo4 from Sulfolobus solfataricus.
abstract: 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.
authors.affiliation: Department of Biochemistry and Center in Molecular Toxicology, Vanderbilt University, Nashville, TN 37232, USA.
authors.forename: Adriana
authors.initials: A
authors.lastname: Irimia
authors.forename: Lioudmila V
authors.initials: LV
authors.lastname: Loukachevitch
authors.forename: Robert L
authors.initials: RL
authors.lastname: Eoff
authors.forename: F Peter
authors.initials: FP
authors.lastname: Guengerich
authors.forename: Martin
authors.initials: M
authors.lastname: Egli
mesh_terms: D055162:Biocatalysis; D002118:Calcium / Q000737:chemistry* / Q000378:metabolism; D020134:Catalytic Domain; D002413:Cations, Divalent / Q000737:chemistry / Q000378:metabolism; D018360:Crystallography, X-Ray; D019951:DNA Polymerase beta / Q000737:chemistry*; D008274:Magnesium / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D011485:Protein Binding; D040681:Structural Homology, Protein; D048229:Sulfolobus solfataricus / Q000201:enzymology*
chemical_list: D002413:Cations, Divalent; D019951:DNA Polymerase beta; D008274:Magnesium; D002118:Calcium
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