4FTX

Crystal structure of Ego3 homodimer

Summary for 4FTX

• Entry DOI: 10.2210/pdb4ftx/pdb
• Related: 4FUW
• Descriptor: Protein SLM4, SUCCINIC ACID (3 entities in total)
• Functional Keywords: ego complex, ego3, tor signaling, protein binding
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Cellular location: Vacuole membrane; Single-pass membrane protein: P38247
• Total number of polymer chains: 2
• Total formula weight: 39004.15

Authors

Zhang, T.,Peli-Gulli, M.P.,Yang, H.,De Virgilio, C.,Ding, J. (deposition date: 2012-06-28, release date: 2012-11-28, Last modification date: 2024-03-20)

Primary citation

Zhang, T.,Peli-Gulli, M.P.,Yang, H.,De Virgilio, C.,Ding, J.
Ego3 functions as a homodimer to mediate the interaction between Gtr1-Gtr2 and Ego1 in the ego complex to activate TORC1.
Structure, 20:2151-2160, 2012

PubMed Abstract: The yeast EGO complex, consisting of Gtr1, Gtr2, Ego1, and Ego3, localizes to the endosomal and vacuolar membranes and plays a pivotal role in cell growth and autophagy regulation through relaying amino acid signals to activate TORC1. Here, we report the crystal structures of a wild-type and a mutant form of Saccharomyces cerevisiae Ego3. Ego3 assumes a homodimeric structure similar to that of the mammalian MP1-p14 heterodimer and the C-terminal domains of the yeast Gtr1-Gtr2 heterodimer, both of which function in TORC1 signaling. Structural and genetic data demonstrate that the unique dimer conformation of Ego3 is essential for the integrity and function of the EGO complex. Structural and functional data also identify a potential binding site for Gtr1-Gtr2. These results suggest a structural conservation of the protein components involved in amino acid signaling to TORC1 and reveal structural insights into the molecular mechanism of Ego3 function in TORC1 signaling.

PubMed: 23123112
DOI: 10.1016/j.str.2012.09.019

Experimental method

X-RAY DIFFRACTION (2.1 Å)