PDBsum entry 5ef5

Signaling protein

PDB id: 5ef5

Contents

Protein chains

1004 a.a.

PDB id:

5ef5

Name:

Signaling protein

Title:

Crystal structure of chaetomium thermophilum raptor

Structure:

Raptor from chaetomium thermophilum. Chain: e, a. Engineered: yes

Source:

Chaetomium thermophilum. Organism_taxid: 209285. Gene: raptor. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Expression_system_cell_line: sf21

Resolution:

4.30Å R-factor: 0.372 R-free: 0.391

Authors:

S.Imseng,E.Sauer,C.H.S.Aylett,D.Boehringer,M.N.Hall,N.Ban,T.Maier

Key ref:

C.H.Aylett et al. (2016). Architecture of human mTOR complex 1. Science, 351, 48-52. PubMed id: 26678875 DOI: 10.1126/science.aaa3870

Date:

23-Oct-15 Release date: 30-Dec-15

Protein chains

No UniProt id for this chain

Struc: 1004 a.a.

DOI no: 10.1126/science.aaa3870

Science 351:48-52 (2016)

PubMed id: 26678875

Architecture of human mTOR complex 1.

C.H.Aylett, E.Sauer, S.Imseng, D.Boehringer, M.N.Hall, N.Ban, T.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 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.