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TitleSAP domain forms a flexible part of DNA aperture in Ku70/80.
Journal, issue, pagesFEBS J, Vol. 288, Issue 14, Page 4382-4393, Year 2021
Publish dateFeb 16, 2021
AuthorsAleš Hnízda / Petr Tesina / Thanh-Binh Nguyen / Zdeněk Kukačka / Lukas Kater / Amanda K Chaplin / Roland Beckmann / David B Ascher / Petr Novák / Tom L Blundell /
PubMed AbstractNonhomologous end joining (NHEJ) is a DNA repair mechanism that religates double-strand DNA breaks to maintain genomic integrity during the entire cell cycle. The Ku70/80 complex recognizes DNA ...Nonhomologous end joining (NHEJ) is a DNA repair mechanism that religates double-strand DNA breaks to maintain genomic integrity during the entire cell cycle. The Ku70/80 complex recognizes DNA breaks and serves as an essential hub for recruitment of NHEJ components. Here, we describe intramolecular interactions of the Ku70 C-terminal domain, known as the SAP domain. Using single-particle cryo-electron microscopy, mass spectrometric analysis of intermolecular cross-linking and molecular modelling simulations, we captured variable positions of the SAP domain depending on DNA binding. The first position was localized at the DNA aperture in the Ku70/80 apo form but was not observed in the DNA-bound state. The second position, which was observed in both apo and DNA-bound states, was found below the DNA aperture, close to the helical arm of Ku70. The localization of the SAP domain in the DNA aperture suggests a function as a flexible entry gate for broken DNA. DATABASES: EM maps have been deposited in EMDB (EMD-11933). Coordinates have been deposited in Protein Data Bank (PDB 7AXZ). Other data are available from corresponding authors upon a request.
External linksFEBS J / PubMed:33511782 / PubMed Central
MethodsEM (single particle)
Resolution3.2 Å
Structure data

11933

7axz

EMDB-11933, PDB-7axz:
Ku70/80 complex apo form
Method: EM (single particle) / Resolution: 3.2 Å

Source
  • homo sapiens (human)
KeywordsDNA BINDING PROTEIN / NHEJ / Ku70/80 / XRCC5 / XRCC6 / DNA damage

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