Journal: Science / Year: 2016 Title: Architecture of human mTOR complex 1. Authors: Christopher H S Aylett / Evelyn Sauer / Stefan Imseng / Daniel Boehringer / Michael N Hall / Nenad Ban / Timm Maier / Abstract: Target of rapamycin (TOR), a conserved protein kinase and central controller of cell growth, functions in two structurally and functionally distinct complexes: TORC1 and TORC2. Dysregulation of ...Target of rapamycin (TOR), a conserved protein kinase and central controller of cell growth, functions in two structurally and functionally distinct complexes: TORC1 and TORC2. Dysregulation of mammalian TOR (mTOR) signaling is implicated in pathologies that include diabetes, cancer, and neurodegeneration. We resolved the architecture of human mTORC1 (mTOR with subunits Raptor and mLST8) bound to FK506 binding protein (FKBP)-rapamycin, by combining cryo-electron microscopy at 5.9 angstrom resolution with crystallographic studies of Chaetomium thermophilum Raptor at 4.3 angstrom resolution. The structure explains how FKBP-rapamycin and architectural elements of mTORC1 limit access to the recessed active site. Consistent with a role in substrate recognition and delivery, the conserved amino-terminal domain of Raptor is juxtaposed to the kinase active site.
History
Deposition
Oct 23, 2015
Deposition site: RCSB / Processing site: PDBE
Revision 1.0
Dec 30, 2015
Provider: repository / Type: Initial release
Revision 1.1
Jan 13, 2016
Group: Database references
Revision 1.2
Apr 24, 2019
Group: Data collection / Source and taxonomy / Category: entity_src_gen / pdbx_seq_map_depositor_info Item: _entity_src_gen.pdbx_host_org_cell_line / _pdbx_seq_map_depositor_info.one_letter_code_mod
Mass: 87589.977 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Chaetomium thermophilum (fungus) / Gene: Raptor / Cell line (production host): Sf21 / Production host: Spodoptera frugiperda (fall armyworm)
Compound details
Due to the the low resolution of the diffraction data, author could not identify the correct ...Due to the the low resolution of the diffraction data, author could not identify the correct numbering/type of the residues. The residue numbering is arbitrary. The one-letter sequence for the protein corresponds to the UniProt accession G0S1S2 (http://www.uniprot.org/uniprot/G0S1S2.fasta)
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION
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Sample preparation
Crystal
Density Matthews: 6.58 Å3/Da / Density % sol: 81.31 %
Crystal grow
Temperature: 303 K / Method: vapor diffusion, sitting drop / pH: 5.3 Details: 3-dimensional Crystals of 0.15 mm - 0.25 mm in size grew within 5-7 days PH range: 5.2-5.4
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