RRC ID 3208
著者 Kobayashi N, Nishino K, Hirata T, Yamaguchi A.
タイトル Membrane topology of ABC-type macrolide antibiotic exporter MacB in Escherichia coli.
ジャーナル 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.
巻・号 546(2-3)
ページ 241-6
公開日 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
引用数 54
WOS 分野 BIOPHYSICS BIOCHEMISTRY & MOLECULAR BIOLOGY CELL BIOLOGY
リソース情報
原核生物(大腸菌) pBAD24 pBAD33