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Structures of the otopetrin proton channels Otop1 and Otop3.

Abstract：

:Otopetrins (Otop1-Otop3) comprise one of two known eukaryotic proton-selective channel families. Otop1 is required for otoconia formation and a candidate mammalian sour taste receptor. Here we report cryo-EM structures of zebrafish Otop1 and chicken Otop3 in lipid nanodiscs. The structures reveal a dimeric architecture, with each subunit forming 12 transmembrane helices divided into structurally similar amino (N) and carboxy (C) domains. Cholesterol-like molecules occupy various sites in Otop1 and Otop3 and occlude a central tunnel. In molecular dynamics simulations, hydrophilic vestibules formed by the N and C domains and in the intrasubunit interface between N and C domains form conduits for water entry into the membrane core, suggesting three potential proton conduction pathways. By mutagenesis, we tested the roles of charged residues in each putative permeation pathway. Our results provide a structural basis for understanding selective proton permeation and gating of this conserved family of proton channels.

journal_name

Nat Struct Mol Biol

journal_title

Nature structural & molecular biology

authors

Saotome K,Teng B,Tsui CCA,Lee WH,Tu YH,Kaplan JP,Sansom MSP,Liman ER,Ward AB

doi

10.1038/s41594-019-0235-9

subject

Has Abstract

pub_date

2019-06-01 00:00:00

pages

518-525

issue

6

eissn

1545-9993

issn

1545-9985

pii

10.1038/s41594-019-0235-9

journal_volume

26

pub_type

杂志文章

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