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PDBsum entry 4zye
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References listed in PDB file
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Key reference
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Title
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Structure-Function relationships governing activity and stability of a DNA alkylation damage repair thermostable protein.
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Authors
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G.Perugino,
R.Miggiano,
M.Serpe,
A.Vettone,
A.Valenti,
S.Lahiri,
F.Rossi,
M.Rossi,
M.Rizzi,
M.Ciaramella.
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Ref.
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Nucleic Acids Res, 2015,
43,
8801-8816.
[DOI no: ]
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PubMed id
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Abstract
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Alkylated DNA-protein alkyltransferases repair alkylated DNA bases, which are
among the most common DNA lesions, and are evolutionary conserved, from
prokaryotes to higher eukaryotes. The human ortholog, hAGT, is involved in
resistance to alkylating chemotherapy drugs. We report here on the alkylated
DNA-protein alkyltransferase, SsOGT, from an archaeal species living at high
temperature, a condition that enhances the harmful effect of DNA alkylation. The
exceptionally high stability of SsOGT gave us the unique opportunity to perform
structural and biochemical analysis of a protein of this class in its
post-reaction form. This analysis, along with those performed on SsOGT in its
ligand-free and DNA-bound forms, provides insights in the structure-function
relationships of the protein before, during and after DNA repair, suggesting a
molecular basis for DNA recognition, catalytic activity and protein
post-reaction fate, and giving hints on the mechanism of alkylation-induced
inactivation of this class of proteins.
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