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4XPM

Crystal structure of EGO-TC

Summary for 4XPM
Entry DOI10.2210/pdb4xpm/pdb
DescriptorProtein MEH1, Uncharacterized protein YCR075W-A, Protein SLM4, ... (4 entities in total)
Functional Keywordsego complex, ego1, ego2, ego3, tor signaling, rapamycin, protein binding
Biological sourceSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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Cellular locationVacuole membrane : Q02205
Vacuole membrane ; Single-pass membrane protein : P38247
Total number of polymer chains3
Total formula weight30890.83
Authors
Powis, K.,Zhang, T.,De Virgilio, C.,Ding, J. (deposition date: 2015-01-17, release date: 2015-08-05, Last modification date: 2023-11-08)
Primary citationPowis, K.,Zhang, T.,Panchaud, N.,Wang, R.,De Virgilio, C.,Ding, J.
Crystal structure of the Ego1-Ego2-Ego3 complex and its role in promoting Rag GTPase-dependent TORC1 signaling.
Cell Res., 25:1043-1059, 2015
Cited by
PubMed Abstract: The target of rapamycin complex 1 (TORC1) integrates various hormonal and nutrient signals to regulate cell growth, proliferation, and differentiation. Amino acid-dependent activation of TORC1 is mediated via the yeast EGO complex (EGOC) consisting of Gtr1, Gtr2, Ego1, and Ego3. Here, we identify the previously uncharacterized Ycr075w-a/Ego2 protein as an additional EGOC component that is required for the integrity and localization of the heterodimeric Gtr1-Gtr2 GTPases, equivalent to mammalian Rag GTPases. We also report the crystal structure of the Ego1-Ego2-Ego3 ternary complex (EGO-TC) at 2.4 Å resolution, in which Ego2 and Ego3 form a heterodimer flanked along one side by Ego1. Structural data also reveal the structural conservation of protein components between the yeast EGO-TC and the human Ragulator, which acts as a GEF for Rag GTPases. Interestingly, however, artificial tethering of Gtr1-Gtr2 to the vacuolar membrane is sufficient to activate TORC1 in response to amino acids even in the absence of the EGO-TC. Our structural and functional data therefore support a model in which the EGO-TC acts as a scaffold for Rag GTPases in TORC1 signaling.
PubMed: 26206314
DOI: 10.1038/cr.2015.86
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

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数据于2024-11-06公开中

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