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Structure paper

TitleThymine DNA glycosylase exhibits negligible affinity for nucleobases that it removes from DNA.
Journal, issue, pagesNucleic Acids Res., Vol. 43, Page 9541-9552, Year 2015
Publish dateDec 23, 2014 (structure data deposition date)
AuthorsMalik, S.S. / Coey, C.T. / Varney, K.M. / Pozharski, E. / Drohat, A.C.
External linksNucleic Acids Res. / PubMed:26358812
MethodsX-ray diffraction
Resolution1.45 - 2.02 Å
Structure data

PDB-4xeg:
Structure of the enzyme-product complex resulting from TDG action on a G/hmU mismatch
Method: X-RAY DIFFRACTION / Resolution: 1.72 Å

PDB-4z3a:
Acetate-free structure of the enzyme-product complex resulting from TDG action on a GU mismatch
Method: X-RAY DIFFRACTION / Resolution: 1.72 Å

PDB-4z47:
Structure of the enzyme-product complex resulting from TDG action on a GU mismatch in the presence of excess base
Method: X-RAY DIFFRACTION / Resolution: 1.45 Å

PDB-4z7b:
Structure of the enzyme-product complex resulting from TDG action on a GfC mismatch
Method: X-RAY DIFFRACTION / Resolution: 2.02 Å

PDB-4z7z:
Structure of the enzyme-product complex resulting from TDG action on a GT mismatch in the presence of excess base
Method: X-RAY DIFFRACTION / Resolution: 1.83 Å

Chemicals

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-ACY:
ACETIC ACID

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • unidentified (others)
  • synthetic construct (others)
KeywordsHYDROLASE/DNA / DNA glycosylase / abasic site / enzyme-product complex / 5-hydroxymethyluracil / HYDROLASE-DNA complex / protein-DNA complex / DNA binding protein/DNA / DNA binding protein-DNA complex

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