3JBZ

Crystal structure of mTOR docked into EM map of dimeric ATM kinase

Summary for 3JBZ

• Entry DOI: 10.2210/pdb3jbz/pdb
• EMDB information: 6501
• Descriptor: Serine/threonine-protein kinase mTOR, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: mtor, pikk, transferase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 134310.39

Authors

Lau, W.C.Y. (deposition date: 2015-11-03, release date: 2016-11-16, Last modification date: 2024-03-20)

Primary citation

Lau, W.C.,Li, Y.,Liu, Z.,Gao, Y.,Zhang, Q.,Huen, M.S.
Structure of the human dimeric ATM kinase.
Cell Cycle, 15:1117-1124, 2016

PubMed Abstract: 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.

PubMed: 27097373
DOI: 10.1080/15384101.2016.1158362

Experimental method

ELECTRON MICROSCOPY (28 Å)