Membrane topology of ABC-type macrolide antibiotic exporter MacB in Escherichia coli

被引：62

作者：

Kobayashi, N

Nishino, K

Hirata, T

Yamaguchi, A

机构：

[1] Osaka Univ, Inst Sci & Ind Res, Dept Cell Membrance Biol, Osaka 5670047, Japan

[2] Osaka Univ, Fac Pharmaceut Sci, Suita, Osaka 5650871, Japan

[3] Japan Sci & Technol Corp, CREST, Osaka 5670047, Japan

来源：

FEBS LETTERS | 2003年 / 546卷 / 2-3期

关键词：

ABC transporter; membrane topology; site-directed mutagenesis; cysteine modification;

D O I：

10.1016/S0014-5793(03)00579-9

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

MacB is an ABC-type membrane protein that exports only macrolide compounds containing 14- and 15-membered lactones, cooperating with a membrane fusion protein, MacA, and a multifunctional outer membrane channel, TolC. We determined the membrane topology of MacB by means of site-specific competitive chemical modification of single cysteine mutants. As a result, it was revealed that MacB is composed of four transmembrane (TM) segments with a cytoplasmic N-terminal nucleotide binding domain of about 270 amino acid residues and a periplasmic large hydrophilic polypeptide between TM segments I and 2 of about 200 amino acid residues. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：241 / 246

页数：6

共 26 条

[1] Molecular cloning and functional analysis of a novel macrolide-resistance determinant, mefA, from Streptococcus pyogenes [J].