Crystal Structure of the Gtr1p(GTP)-Gtr2p(GDP) Protein Complex Reveals Large Structural Rearrangements Triggered by GTP-to-GDP Conversion

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The heterodimeric Rag GTPases consisting of RagA (or RagB) and RagC (or RagD) are the key regulator activating the target of rapamycin complex 1 (TORC1) in response to the level of amino acids. The heterodimer between GTP-loaded RagA/B and GDP-loaded RagC/D is the most active form that binds Raptor and leads to the activation of TORC1. Here, we present the crystal structure of Gtr1pGTP-Gtr2pGDP, the active yeast Rag GTPase heterodimer. The structure reveals that GTP-to-GDP conversion on Gtr2p results in a large conformational transition of this subunit, including a large scale rearrangement of a long segment whose corresponding region in RagA is involved in binding to Raptor. In addition, the two GTPase domains of the heterodimer are brought to contact with each other, but without causing any conformational change of the Gtr1p subunit. These features explain how the nucleotide-bound statuses of the two GTPases subunits switch the Raptor binding affinity on and off.
Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Issue Date
2012-08
Language
English
Article Type
Article
Keywords

BINDING PROTEINS; RAG GTPASES; ACTIVATION; TORC1; HYDROLYSIS; MTORC1

Citation

JOURNAL OF BIOLOGICAL CHEMISTRY, v.287, no.35, pp.29648 - 29653

ISSN
0021-9258
DOI
10.1074/jbc.C112.384420
URI
http://hdl.handle.net/10203/103009
Appears in Collection
BS-Journal Papers(저널논문)
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