Open AccessMetal‐ion dependence of the active‐site conformation of the translesion DNA polymerase Dpo4 from Sulfolobus solfataricus
Author(s) -
Irimia Adriana,
Loukachevitch Lioudmila V.,
Eoff Robert L.,
Guengerich F. Peter,
Egli Martin
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110029374
Subject(s) - sulfolobus solfataricus , dna polymerase , dna , dna polymerase beta , chemistry , dna clamp , polymerase , stereochemistry , active site , crystallography , biochemistry , dna damage , enzyme , polymerase chain reaction , gene , base excision repair , reverse transcriptase , archaea
Crystal structures of a binary Mg 2+ ‐form Dpo4–DNA complex with 1, N 2 ‐etheno‐dG in the template strand as well as of ternary Mg 2+ ‐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 Ca 2+ ‐form complexes revealed that the DNA and polymerase undergo subtle changes as a result of the catalytically more active Mg 2+ occupying both the A and B sites.