Ion channel formation by N-terminal domain:: a common feature of OprFs of Pseudomonas and OmpA of Escherichia coli

被引：25

作者：

Saint, N ^{[1
]}

El Hamel, C ^{[1
]}

Dé, E ^{[1
]}

Molle, G ^{[1
]}

机构：

[1] Univ Rouen, Fac Sci, IFRMP 23, UMR 6522 CNRS, F-76821 Mt St Aignan, France

来源：

FEMS MICROBIOLOGY LETTERS | 2000年 / 190卷 / 02期

关键词：

lipid bilayer; porin; outer membrane; beta-barrel;

D O I：

10.1016/S0378-1097(00)00345-1

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The proteolytic fragments of OprFs of Pseudomonas aeruginosa and Pseudomonas fluorescens were identified, respectively, as the first 175 and 177 amino acids from the N-terminal domain. They induced ion channels after reincorporation into planar lipid bilayers (85 and 75 pS, respectively, in 1 M NaCl). A similar conductance value (72 pS) was found for the eight beta-strand OmpA N-terminal domain (OmpA(171)) of Escherichia coli. We conclude that the N-terminal domain of OprFs is sufficient to induce ion channels and the comparison with OmpA(171), provides strong evidence of the existence of an eight-stranded beta-barrel in the N-terminal domain of OprFs. (C) 2000 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：261 / 265

页数：5

共 23 条

[1] Refolded outer membrane protein A of Escherichia coli forms ion channels with two conductance states in planar lipid bilayers [J].