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FEBS Lett. 2003 Jul 10;546(2-3):241-6.

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

Author information

1
Department of Cell Membrane Biology, Institute of Scientific and Industrial Research, Osaka University, 8-1 Mihogaoka, Ibaraki, Osaka 567-0047, Japan.

Abstract

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 1 and 2 of about 200 amino acid residues.

PMID:
12832048
DOI:
10.1016/s0014-5793(03)00579-9
[Indexed for MEDLINE]
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