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6SYT

Structure of the SMG1-SMG8-SMG9 complex

Summary for 6SYT
Entry DOI10.2210/pdb6syt/pdb
EMDB information10347
DescriptorSMG1,Serine/threonine-protein kinase SMG1,SMG1,Serine/threonine-protein kinase SMG1,SMG1,Serine/threonine-protein kinase SMG1,SMG1,Serine/threonine-protein kinase SMG1,SMG1,Serine/threonine-protein kinase SMG1, Protein SMG8, Protein SMG9, ... (6 entities in total)
Functional Keywordskinase, nmd, ip6, g-fold protein, pikk family, signaling protein
Biological sourceHomo sapiens
More
Total number of polymer chains3
Total formula weight570138.68
Authors
Gat, Y.,Schuller, J.M.,Conti, E. (deposition date: 2019-10-01, release date: 2019-12-11, Last modification date: 2024-05-22)
Primary citationGat, Y.,Schuller, J.M.,Lingaraju, M.,Weyher, E.,Bonneau, F.,Strauss, M.,Murray, P.J.,Conti, E.
InsP6binding to PIKK kinases revealed by the cryo-EM structure of an SMG1-SMG8-SMG9 complex.
Nat.Struct.Mol.Biol., 26:1089-1093, 2019
Cited by
PubMed Abstract: We report the 3.45-Å resolution cryo-EM structure of human SMG1-SMG8-SMG9, a phosphatidylinositol-3-kinase (PI(3)K)-related protein kinase (PIKK) complex central to messenger RNA surveillance. Structural and MS analyses reveal the presence of inositol hexaphosphate (InsP) in the SMG1 kinase. We show that the InsP-binding site is conserved in mammalian target of rapamycin (mTOR) and potentially other PIKK members, and that it is required for optimal in vitro phosphorylation of both SMG1 and mTOR substrates.
PubMed: 31792449
DOI: 10.1038/s41594-019-0342-7
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.45 Å)
Structure validation

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