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TitleStructures of closed and open conformations of dimeric human ATM.
Journal, issue, pagesSci Adv, Vol. 3, Issue 5, Page e1700933, Year 2017
Publish dateMay 10, 2017
AuthorsDomagoj Baretić / Hannah K Pollard / David I Fisher / Christopher M Johnson / Balaji Santhanam / Caroline M Truman / Tomas Kouba / Alan R Fersht / Christopher Phillips / Roger L Williams /
PubMed AbstractATM (ataxia-telangiectasia mutated) is a phosphatidylinositol 3-kinase-related protein kinase (PIKK) best known for its role in DNA damage response. ATM also functions in oxidative stress response, ...ATM (ataxia-telangiectasia mutated) is a phosphatidylinositol 3-kinase-related protein kinase (PIKK) best known for its role in DNA damage response. ATM also functions in oxidative stress response, insulin signaling, and neurogenesis. Our electron cryomicroscopy (cryo-EM) suggests that human ATM is in a dynamic equilibrium between closed and open dimers. In the closed state, the PIKK regulatory domain blocks the peptide substrate-binding site, suggesting that this conformation may represent an inactive or basally active enzyme. The active site is held in this closed conformation by interaction with a long helical hairpin in the TRD3 (tetratricopeptide repeats domain 3) domain of the symmetry-related molecule. The open dimer has two protomers with only a limited contact interface, and it lacks the intermolecular interactions that block the peptide-binding site in the closed dimer. This suggests that the open conformation may be more active. The ATM structure shows the detailed topology of the regulator-interacting N-terminal helical solenoid. The ATM conformational dynamics shown by the structures represent an important step in understanding the enzyme regulation.
External linksSci Adv / PubMed:28508083 / PubMed Central
MethodsEM (single particle)
Resolution4.4 - 11.5 Å
Structure data

EMDB-3668:
Closed dimer (C2) of human ATM (Ataxia telangiectasia mutated)
Method: EM (single particle) / Resolution: 4.7 Å

EMDB-3669: Closed dimer (C1) of human ATM (Ataxia telangiectasia mutated)
PDB-5np0: Closed dimer of human ATM (Ataxia telangiectasia mutated)
Method: EM (single particle) / Resolution: 5.7 Å

EMDB-3670:
Closed dimer Pincer-FATKIN of human ATM (Ataxia telangiectasia mutated)
Method: EM (single particle) / Resolution: 4.4 Å

EMDB-3671:
Open dimer of human ATM (Ataxia telangiectasia mutated)
Method: EM (single particle) / Resolution: 11.5 Å

EMDB-3672, PDB-5np1:
Open protomer of human ATM (Ataxia telangiectasia mutated)
Method: EM (single particle) / Resolution: 5.7 Å

EMDB-3673:
Open protomer Pincer-FATKIN of human ATM (Ataxia telangiectasia mutated)
Method: EM (single particle) / Resolution: 4.8 Å

Source
  • homo sapiens (human)
KeywordsSIGNALING PROTEIN / PIKK / kinase / DNA-repair / HEAT-repeats / TRANSFERASE / FAT / MRN

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