期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 287, 期 35, 页码 29648-29653出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.C112.384420
关键词
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资金
- Marine Extreme Genome Research Center Program of the Ministry of Land, Transport and Maritime Affairs
- Basic Science Research Program through National Research Foundation of Korea (NRF)
- Ministry of Education, Science and Technology [2011-0007201]
- Global Research Laboratory (GRL) Program, NRF of Korea [K20815000001]
- American Diabetes Association [7-07-CD-08]
- National Institutes of Health [DK072004, DK083474]
- National Research Foundation of Korea [2011-0007201] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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.
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