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Structure paper

TitleThermococcus kodakarensis TK0353 is a novel AP lyase with a new fold.
Journal, issue, pagesJ. Biol. Chem., Vol. 300, Page 105503-105503, Year 2023
Publish dateMar 24, 2023 (structure data deposition date)
AuthorsCaffrey, P.J. / Eckenroth, B.E. / Burkhart, B.W. / Zatopek, K.M. / McClung, C.M. / Santangelo, T.J. / Doublie, S. / Gardner, A.F.
External linksJ. Biol. Chem. / PubMed:38013090
MethodsX-ray diffraction
Resolution1.75 - 2.2 Å
Structure data

PDB-8gm6:
Structure of apurinic/apyrimidinic DNA lyase TK0353 from Thermococcus kodakarensis (Selenomethionine)
Method: X-RAY DIFFRACTION / Resolution: 1.98 Å

PDB-8gm7:
Structure of apurinic/apyrimidinic DNA Lyase TK0353 from Thermococcus kodakarensis (Native Crystal Form)
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

PDB-8syj:
Structure of apurinic/apyrimidinic DNA lyase TK0353 from Thermococcus kodakarensis (Iodide crystal form)
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-IOD:
IODIDE ION

Source
  • thermococcus kodakarensis (archaea)
KeywordsLYASE / apurinic/apyrimidinic DNA lyase DNA binding protein / DNA binding apurinic/apyrimidinic DNA lyase

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