Reference - Detail
| RRC ID | 3208 |
|---|---|
| Author | Kobayashi N, Nishino K, Hirata T, Yamaguchi A. |
| Title | Membrane topology of ABC-type macrolide antibiotic exporter MacB in Escherichia coli. |
| Journal | FEBS Lett |
| 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. |
| Volume | 546(2-3) |
| Pages | 241-6 |
| Published | 2003-7-10 |
| DOI | 10.1016/s0014-5793(03)00579-9 |
| PII | S0014579303005799 |
| PMID | 12832048 |
| MeSH | 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 |
| IF | 3.057 |
| Times Cited | 54 |
| WOS Category | BIOPHYSICS BIOCHEMISTRY & MOLECULAR BIOLOGY CELL BIOLOGY |
| Resource | |
| Prokaryotes E. coli | pBAD24 pBAD33 |