3LGO

Structure of Gse1p, member of the GSE/EGO complex

3LGO の概要

• エントリーDOI: 10.2210/pdb3lgo/pdb
• 分子名称: Protein SLM4 (2 entities in total)
• 機能のキーワード: roadblock/lc7, domain swap, autophagy, membrane, transmembrane, transport, vacuole, protein binding
• 由来する生物種: Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast)
• 細胞内の位置: Vacuole membrane; Single-pass membrane protein: P38247
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19563.16

構造登録者

Kogan, K.,Fass, D. (登録日: 2010-01-21, 公開日: 2010-08-04, 最終更新日: 2024-02-21)

主引用文献

Kogan, K.,Spear, E.D.,Kaiser, C.A.,Fass, D.
Structural conservation of components in the amino acid sensing branch of the TOR pathway in yeast and mammals.
J.Mol.Biol., 402:388-398, 2010

PubMed Abstract: The highly conserved Rag family GTPases have a role in reporting amino acid availability to the TOR (target of rapamycin) signaling complex, which regulates cell growth and metabolism in response to environmental cues. The yeast Rag proteins Gtr1p and Gtr2p were shown in multiple independent studies to interact with the membrane-associated proteins Gse1p (Ego3p) and Gse2p (Ego1p). However, mammalian orthologs of Gse1p and Gse2p could not be identified. We determined the crystal structure of Gse1p and found it to match the fold of two mammalian proteins, MP1 (mitogen-activated protein kinase scaffold protein 1) and p14, which form a heterodimeric complex that had been assigned a scaffolding function in mitogen-activated protein kinase pathways. The significance of this structural similarity is validated by the recent identification of a physical and functional association between mammalian Rag proteins and MP1/p14. Together, these findings reveal that key components of the TOR signaling pathway are structurally conserved between yeast and mammals, despite divergence of sequence to a degree that thwarts detection through simple homology searches.

PubMed: 20655927
DOI: 10.1016/j.jmb.2010.07.034

実験手法

X-RAY DIFFRACTION (2.85 Å)