4ARZ

The crystal structure of Gtr1p-Gtr2p complexed with GTP-GDP

Summary for 4ARZ

• Entry DOI: 10.2210/pdb4arz/pdb
• Descriptor: GTP-BINDING PROTEIN GTR1, GTP-BINDING PROTEIN GTR2, GUANOSINE-5'-TRIPHOSPHATE, ... (6 entities in total)
• Functional Keywords: hydrolase, gtpase, cell growth
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); More
• Cellular location: Vacuole membrane: Q00582 P53290
• Total number of polymer chains: 2
• Total formula weight: 75517.11

Authors

Jeong, J.H.,Kim, Y.G. (deposition date: 2012-04-27, release date: 2012-07-25, Last modification date: 2024-05-08)

Primary citation

Jeong, J.H.,Lee, K.H.,Kim, Y.M.,Kim, D.H.,Oh, B.H.,Kim, Y.G.
Crystal Structure of the Gtr1Pgtp-Gtr2Pgdp Complex Reveals Large Structural Rearrangements Triggered by GTP-to-Gdp Conversion
J.Biol.Chem., 287:29648-, 2012

PubMed Abstract: 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 Gtr1p(GTP)-Gtr2p(GDP), 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.

PubMed: 22807443
DOI: 10.1074/JBC.C112.384420

Experimental method

X-RAY DIFFRACTION (3.1 Å)