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TitleStructure of the human dimeric ATM kinase.
Journal, issue, pagesCell Cycle, Vol. 15, Issue 8, Page 1117-1124, Year 2016
Publish dateJan 6, 2017
AuthorsWilson C Y Lau / Yinyin Li / Zhe Liu / Yuanzhu Gao / Qinfen Zhang / Michael S Y Huen /
PubMed AbstractDNA-double strand breaks activate the serine/threonine protein kinase ataxia-telangiectasia mutated (ATM) to initiate DNA damage signal transduction. This activation process involves ...DNA-double strand breaks activate the serine/threonine protein kinase ataxia-telangiectasia mutated (ATM) to initiate DNA damage signal transduction. This activation process involves autophosphorylation and dissociation of inert ATM dimers into monomers that are catalytically active. Using single-particle electron microscopy (EM), we determined the structure of dimeric ATM in its resting state. The EM map could accommodate the crystal structure of the N-terminal truncated mammalian target of rapamycin (mTOR), a closely related enzyme of the phosphatidylinositol 3-kinase-related protein kinase (PIKK) family, allowing for the localization of the N- and the C-terminal regions of ATM. In the dimeric structure, the actives sites are buried, restricting the access of the substrates to these sites. The unanticipated domain organization of ATM provides a basis for understanding its mechanism of inhibition.
External linksCell Cycle / PubMed:27097373 / PubMed Central
MethodsEM (single particle)
Resolution28.0 Å
Structure data

EMDB-6499:
Structural insights into the regulatory mechanism of ATM kinase activation
Method: EM (single particle) / Resolution: 28.0 Å

6501

3jbz

EMDB-6501: Electron microscopy of dimeric ATM kinase
PDB-3jbz: Crystal structure of mTOR docked into EM map of dimeric ATM kinase
Method: EM (single particle) / Resolution: 28.0 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

ChemComp-MGF:
TRIFLUOROMAGNESATE

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / mTOR / PIKK

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