5OYK

Outer-membrane expressed OmpT of Vibrio cholerae

5OYK の概要

• エントリーDOI: 10.2210/pdb5oyk/pdb
• 分子名称: Gram-negative porin family protein (1 entity in total)
• 機能のキーワード: outer membrane protein, porin, ompf or ompc ortholog, ion-transport, membrane beta barrel, ion-channel, membrane protein
• 由来する生物種: Vibrio cholerae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35424.59

構造登録者

van den berg, B.,Pathania, M. (登録日: 2017-09-11, 公開日: 2018-04-25, 最終更新日: 2024-01-17)

主引用文献

Pathania, M.,Acosta-Gutierrez, S.,Bhamidimarri, S.P.,Basle, A.,Winterhalter, M.,Ceccarelli, M.,van den Berg, B.
Unusual Constriction Zones in the Major Porins OmpU and OmpT from Vibrio cholerae.
Structure, 26:708-721.e4, 2018

PubMed Abstract: The outer membranes (OM) of many Gram-negative bacteria contain general porins, which form nonspecific, large-diameter channels for the diffusional uptake of small molecules required for cell growth and function. While the porins of Enterobacteriaceae (e.g., E. coli OmpF and OmpC) have been extensively characterized structurally and biochemically, much less is known about their counterparts in Vibrionaceae. Vibrio cholerae, the causative agent of cholera, has two major porins, OmpU and OmpT, for which no structural information is available despite their importance for the bacterium. Here we report high-resolution X-ray crystal structures of V. cholerae OmpU and OmpT complemented with molecular dynamics simulations. While similar overall to other general porins, the channels of OmpU and OmpT have unusual constrictions that create narrower barriers for small-molecule permeation and change the internal electric fields of the channels. Together with electrophysiological and in vitro transport data, our results illuminate small-molecule uptake within the Vibrionaceae.

PubMed: 29657131
DOI: 10.1016/j.str.2018.03.010

実験手法

X-RAY DIFFRACTION (3.2 Å)