PDBsum entry 5flc

Transferase

PDB id: 5flc

Contents

Protein chains

615 a.a.

365 a.a.

1029 a.a.

1050 a.a.

107 a.a.

317 a.a.

Ligands

RAP ×2

PDB id:

5flc

Name:

Transferase

Title:

Architecture of human mtor complex 1 - 5.9 angstrom reconstruction

Structure:

Serine/threonine-protein kinase mtor. Chain: 1, 3. Fragment: horn domain. Synonym: fk506-binding protein 12-rapamycin complex-associated protein 1, fkbp12-rapamycin complex-associated protein, mammalian target of rapamycin, mtor, mechanistic target of rapamycin, rapamycin and fkbp12 target 1, rapamycin target protein 1. Engineered: yes. Serine/threonine-protein kinase mtor.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Expression_system_cell_line: sf21. Spodoptera frugiperda. Fall armyworm. Organism_taxid: 7108.

Authors:

C.H.S.Aylett,E.Sauer,S.Imseng,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: 615 a.a.

Protein chains

No UniProt id for this chain

Struc: 365 a.a.

Protein chains

No UniProt id for this chain

Struc: 1029 a.a.

Protein chains

P42345  (MTOR_HUMAN) -  Serine/threonine-protein kinase mTOR from Homo sapiens

Seq: 2549 a.a.

Struc: 1050 a.a.

Protein chains

No UniProt id for this chain

Struc: 107 a.a.

Protein chains

Q9BVC4  (LST8_HUMAN) -  Target of rapamycin complex subunit LST8 from Homo sapiens

Seq: 326 a.a.

Struc: 317 a.a.

Enzyme reactions

• Enzyme class 1: Chains B, F: E.C.2.7.11.1 - non-specific serine/threonine protein kinase.
• Reaction:
  1. L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H⁺
  2. L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H⁺
• Enzyme class 2: Chains D, H: E.C.?

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

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.