7V74

Thermostabilized human prestin in complex with sulfate

7V74 の概要

• エントリーDOI: 10.2210/pdb7v74/pdb
• EMDBエントリー: 31758
• 分子名称: prestin, SULFATE ION, CHOLESTEROL, ... (4 entities in total)
• 機能のキーワード: motor protein, prestin, slc26a5, electromotility, membrane protein
• 由来する生物種: Homo sapiens
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 89453.35

構造登録者

Futamata, H.,Fukuda, M.,Yamashita, K.,Nishizawa, T.,Nureki, O. (登録日: 2021-08-21, 公開日: 2022-08-31, 最終更新日: 2024-06-12)

主引用文献

Futamata, H.,Fukuda, M.,Umeda, R.,Yamashita, K.,Tomita, A.,Takahashi, S.,Shikakura, T.,Hayashi, S.,Kusakizako, T.,Nishizawa, T.,Homma, K.,Nureki, O.
Cryo-EM structures of thermostabilized prestin provide mechanistic insights underlying outer hair cell electromotility.
Nat Commun, 13:6208-6208, 2022

PubMed Abstract: Outer hair cell elecromotility, driven by prestin, is essential for mammalian cochlear amplification. Here, we report the cryo-EM structures of thermostabilized prestin (Pres), complexed with chloride, sulfate, or salicylate at 3.52-3.63 Å resolutions. The central positively-charged cavity allows flexible binding of various anion species, which likely accounts for the known distinct modulations of nonlinear capacitance (NLC) by different anions. Comparisons of these Pres structures with recent prestin structures suggest rigid-body movement between the core and gate domains, and provide mechanistic insights into prestin inhibition by salicylate. Mutations at the dimeric interface severely diminished NLC, suggesting that stabilization of the gate domain facilitates core domain movement, thereby contributing to the expression of NLC. These findings advance our understanding of the molecular mechanism underlying mammalian cochlear amplification.

PubMed: 36266333
DOI: 10.1038/s41467-022-34017-x

実験手法

ELECTRON MICROSCOPY (3.63 Å)