Open AccessThe MalK protein of the ATP-binding cassette transporter for maltose of Escherichia coli is accessible to protease digestion from the periplasmic side of the membrane
Author(s) -
Erwin Schneider,
Sabine Hunke,
Sandra Tebbe
Publication year - 1995
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.177.18.5364-5367.1995
Subject(s) - periplasmic space , atp binding cassette transporter , biology , escherichia coli , biochemistry , maltose binding protein , protein subunit , transmembrane protein , membrane protein , transporter , protease , membrane transport protein , proteinase k , chemiosmosis , enzyme , membrane , atp synthase , gene , fusion protein , receptor , recombinant dna
The ATP-hydrolyzing subunit MalK of the ATP-binding cassette transporter for maltose of Escherichia coli is demonstrated to be accessible to digestion by proteinase K in right-side-out membrane vesicles. This finding suggests a partial transmembrane orientation of the protein.