PMID:12832048
| Citation |
Kobayashi, N, Nishino, K, Hirata, T and Yamaguchi, A (2003) Membrane topology of ABC-type macrolide antibiotic exporter MacB in Escherichia coli. FEBS Lett. 546:241-6 |
|---|---|
| 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. |
| Links | |
| Keywords |
ATP-Binding Cassette Transporters/chemistry; ATP-Binding Cassette Transporters/genetics; ATP-Binding Cassette Transporters/metabolism; Amino Acid Sequence; Carbon Radioisotopes; Cell Membrane/chemistry; Escherichia coli/chemistry; Escherichia coli/genetics; Escherichia coli Proteins; Ethylmaleimide/metabolism; Molecular Sequence Data; Radioligand Assay |
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