Topological analysis of an RND family transporter, MexD ofPseudomonas aeruginosa
| Autor: | Takaomi Wada, Takeshi Nishino, Hideto Tsujimoto, Naomasa Gotoh, Toshiyuki Kusumi |
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| Rok vydání: | 1999 |
| Předmět: |
Protein Conformation
Recombinant Fusion Proteins Blotting Western Molecular Sequence Data Biophysics Biology medicine.disease_cause Topology Models Biological Biochemistry Protein Structure Secondary beta-Lactamases Plasmid Structural Biology Resistance-nodulation-division family Genetics medicine Computer Simulation Amino Acid Sequence Molecular Biology Pseudomonas aeruginosa Membrane Proteins Biological Transport Transporter Cell Biology Periplasmic space Alkaline Phosphatase Transmembrane protein Transmembrane domain Cytoplasm Membrane topology Multidrug efflux MexD Carrier Proteins Bacterial Outer Membrane Proteins Plasmids |
| Zdroj: | FEBS Letters. 458:32-36 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/s0014-5793(99)01116-3 |
| Popis: | The membrane topology of a resistance-nodulation-division (RND) family transporter, MexD of Pseudomonas aeruginosa, was determined. Although it had been predicted previously that most RND proteins contain 12 transmembrane helices, three independent computer programs used in the present study predicted that MexD possessed 11, 14 or 17 transmembrane segments. To investigate the topology of MexD more thoroughly, 25 MexD-PhoA (alkaline phosphatase) and 18 MexD-Bla (β-lactamase) fusion plasmids were constructed and analyzed. The resulting topological model had just 12 transmembrane helices and two periplasmic loops of about 300 residues between helices 1 and 2 and helices 7 and 8. It is therefore proposed that the N- and C-termini are located in the cytoplasm and the predicted orientation is consistent with the ‘positive-inside rule’. This topological model can be applied to other RND proteins. |
| Databáze: | OpenAIRE |
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