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

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...

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Veröffentlicht in:	FEBS letters 2003-07, Vol.546 (2), p.241-246
Hauptverfasser:	Kobayashi, Nobuyoshi, Nishino, Kunihiko, Hirata, Takahiro, Yamaguchi, Akihito
Format:	Artikel
Sprache:	eng
Schlagworte:	ABC transporter ABC, ATP binding cassette Amino Acid Sequence AMS, 4-acetoamide-4′-maleimidylstilbene-2,2′-disulfonic acid ATP-Binding Cassette Transporters - chemistry ATP-Binding Cassette Transporters - genetics ATP-Binding Cassette Transporters - metabolism Carbon Radioisotopes Cell Membrane - chemistry Cysteine modification Escherichia coli Escherichia coli - chemistry Escherichia coli - genetics Escherichia coli Proteins Ethylmaleimide - metabolism MacB protein macrolide antibiotics Membrane topology Molecular Sequence Data NBD, nucleotide binding domain NEM, N-ethyl maleimide Radioligand Assay Site-directed mutagenesis TM, transmembrane topology
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Zusammenfassung:	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.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/S0014-5793(03)00579-9