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-Structure paper
Title | Structure of TOR and its complex with KOG1. |
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Journal, issue, pages | Mol Cell, Vol. 27, Issue 3, Page 509-516, Year 2007 |
Publish date | Aug 3, 2007 |
Authors | Alessandra Adami / Begoña García-Alvarez / Ernesto Arias-Palomo / David Barford / Oscar Llorca / |
PubMed Abstract | The target of rapamycin (TOR) is a large (281 kDa) conserved Ser/Thr protein kinase that functions as a central controller of cell growth. TOR assembles into two distinct multiprotein complexes: ...The target of rapamycin (TOR) is a large (281 kDa) conserved Ser/Thr protein kinase that functions as a central controller of cell growth. TOR assembles into two distinct multiprotein complexes: TORC1 and TORC2. A defining feature of TORC1 is the interaction of TOR with KOG1 (Raptor in mammals) and its sensitivity to a rapamycin-FKBP12 complex. Here, we have reconstructed in three dimensions the 25 A resolution structures of endogenous budding yeast TOR1 and a TOR-KOG1 complex, using electron microscopy. TOR features distinctive N-terminal HEAT repeats that form a curved tubular-shaped domain that associates with the C-terminal WD40 repeat domain of KOG1. The N terminus of KOG1 is in proximity to the TOR kinase domain, likely functioning to bring substrates into the vicinity of the catalytic region. A model is proposed for the molecular architecture of the TOR-KOG1 complex explaining its sensitivity to rapamycin. |
External links | Mol Cell / PubMed:17679098 |
Methods | EM (single particle) |
Resolution | 25.0 - 26.0 Å |
Structure data | EMDB-1360: EMDB-1361: |
Source |
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