Membrane topology of the Escherichia coli ExbD protein
| Autor: | Volkmar Braun, K Kampfenkel |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
DNA
Bacterial Protein Conformation Molecular Sequence Data Biology Microbiology beta-Lactamases Protein structure Bacterial Proteins Escherichia coli Molecular Biology Base Sequence Escherichia coli Proteins Cell Membrane Biological Transport Drug Resistance Microbial Periplasmic space Membrane transport Transmembrane domain Membrane protein Biochemistry Genes Bacterial Membrane topology Colicin Autoradiography Ampicillin Bacterial outer membrane Research Article Plasmids |
| Zdroj: | Journal of Bacteriology. 174:5485-5487 |
| ISSN: | 1098-5530 0021-9193 |
| DOI: | 10.1128/jb.174.16.5485-5487.1992 |
| Popis: | The ExbD protein is involved in the energy-coupled transport of ferric siderophores, vitamin B12, and B-group colicins across the outer membrane of Escherichia coli. In order to study ExbD membrane topology, ExbD-beta-lactamase fusion proteins were constructed. Cells expressing beta-lactamase fusions to residues 53, 57, 70, 76, 78, 80, 92, 121, and 134 of ExbD displayed high levels of ampicillin resistance, whereas fusions to residues 9 and 19 conferred no ampicillin resistance. It is concluded that the only hydrophobic segment of ExbD, encompassing residues 23 to 43, forms a transmembrane domain and that residues 1 to 22 are located in the cytoplasm and residues 44 to 141 are located in the periplasm. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|