EMD-38930

Single-particle
2.83 Å
EMD-38930 Deposition: 31/01/2024
Map released: 29/01/2025
Last modified: 29/01/2025
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-38930

Cryo-EM reveals cholesterol binding in the lysosomal GPCR-like protein LYCHOS

EMD-38930

Single-particle
2.83 Å
EMD-38930 Deposition: 31/01/2024
Map released: 29/01/2025
Last modified: 29/01/2025
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Homo sapiens
Sample: Cholesterol-bound LYCHOS
Fitted models: 8y56

Deposition Authors: Zhao J , Shen QY, Zhang Y , Shao ZH
Cryo-EM reveals cholesterol binding in the lysosomal GPCR-like protein LYCHOS.
Zhao J , Shen Q , Yong X , Li X, Tian X, Sun S, Xu Z , Zhang X, Zhang L, Yang H , Shao Z , Xu H , Jiang Y , Zhang Y , Yan W
(2025) Nat Struct Mol Biol
PUBMED: 39824976
DOI: doi:10.1038/s41594-024-01470-9
ISSN: 1545-9985
Abstract:
Cholesterol plays a pivotal role in modulating the activity of mechanistic target of rapamycin complex 1 (mTOR1), thereby regulating cell growth and metabolic homeostasis. LYCHOS, a lysosome-localized G-protein-coupled receptor-like protein, emerges as a cholesterol sensor and is capable of transducing the cholesterol signal to affect the mTORC1 function. However, the precise mechanism by which LYCHOS recognizes cholesterol remains unknown. Here, using cryo-electron microscopy, we determined the three-dimensional structural architecture of LYCHOS in complex with cholesterol molecules, revealing a unique arrangement of two sequential structural domains. Through a comprehensive analysis of this structure, we elucidated the specific structural features of these two domains and their collaborative role in the process of cholesterol recognition by LYCHOS.