7YR5

Embigin facilitates monocarboxylate transporter 1 localization to plasma membrane and transition to a decoupling state

7YR5 の概要

• エントリーDOI: 10.2210/pdb7yr5/pdb
• EMDBエントリー: 34046
• 分子名称: Embigin, Monocarboxylate transporter 1 (2 entities in total)
• 機能のキーワード: mct1, embigin, membrane protein
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 92019.86

構造登録者

Xu, B.,Ye, S. (登録日: 2022-08-08, 公開日: 2022-09-28, 最終更新日: 2024-10-16)

主引用文献

Xu, B.,Zhang, M.,Zhang, B.,Chi, W.,Ma, X.,Zhang, W.,Dong, M.,Sheng, L.,Zhang, Y.,Jiao, W.,Shan, Y.,Chang, W.,Wang, P.,Wen, S.,Pei, D.,Chen, L.,Zhang, X.,Yan, H.,Ye, S.
Embigin facilitates monocarboxylate transporter 1 localization to the plasma membrane and transition to a decoupling state.
Cell Rep, 40:111343-111343, 2022

PubMed Abstract: Cell-surface ancillary glycoproteins basigin or embigin form heterodimeric complexes with proton-coupled monocarboxylate transporters (MCTs), facilitating the membrane trafficking of MCTs and regulating their transport activities. Here, we determine the cryoelectron microscopy (cryo-EM) structure of the human MCT1-embigin complex and observe that embigin forms extensive interactions with MCT1 to facilitate its localization to the plasma membrane. In addition, the formation of the heterodimer effectively blocks MCT1 from forming a homodimer through a steric hindrance effect, releasing the coupling between two signature motifs and driving a significant conformation change in transmembrane helix 5 (TM5) of MCTs. Consequently, the substrate-binding pocket alternates between states of homodimeric coupling and heterodimeric decoupling states and exhibits differences in substrate-binding affinity, supporting the hypothesis that the substrate-induced motion originating in one subunit of the MCT dimer could be transmitted to the adjacent subunit to alter its substrate-binding affinity.

PubMed: 36103816
DOI: 10.1016/j.celrep.2022.111343

実験手法

ELECTRON MICROSCOPY (3.63 Å)