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TitleStructural comparison of AP endonucleases from the exonuclease III family reveals new amino acid residues in human AP endonuclease 1 that are involved in incision of damaged DNA.
Journal, issue, pagesBiochimie, Vol. 128-129, Page 20-33, Year 2016
Publish dateJul 8, 2015 (structure data deposition date)
AuthorsRedrejo-Rodriguez, M. / Vigouroux, A. / Mursalimov, A. / Grin, I. / Alili, D. / Koshenov, Z. / Akishev, Z. / Maksimenko, A. / Bissenbaev, A.K. / Matkarimov, B.T. ...Redrejo-Rodriguez, M. / Vigouroux, A. / Mursalimov, A. / Grin, I. / Alili, D. / Koshenov, Z. / Akishev, Z. / Maksimenko, A. / Bissenbaev, A.K. / Matkarimov, B.T. / Saparbaev, M. / Ishchenko, A.A. / Morera, S.
External linksBiochimie / PubMed:27343627
MethodsX-ray diffraction
Resolution1.8 - 1.84 Å
Structure data

PDB-5cfe:
Bacillus subtilis AP endonuclease ExoA
Method: X-RAY DIFFRACTION / Resolution: 1.84 Å

PDB-5cfg:
C2 crystal form of APE1 with Mg2+
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-HOH:
WATER

ChemComp-MG:
Unknown entry

Source
  • bacillus subtilis (strain 168) (bacteria)
  • homo sapiens (human)
KeywordsHYDROLASE / AP endonuclease / LYASE

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