Abstract
EmrE is a multidrug transporter from Escherichia coli that belongs to the Smr family of small multidrug transporters. The secondary structure of EmrE consists of a four helical bundle, as judged by different techniques. EmrE has been extensively characterized; nevertheless, the membrane topology of EmrE has not been determined yet. Previous work with a homologous Smr protein provided partial information of the membrane topology, however the location of the carboxy-terminus remained inconclusive. In this work we probed the membrane topology of EmrE, focusing on the carboxy-terminus of the protein, using two independent approaches. Our results support a secondary structure where the carboxy-terminus faces the cytoplasm, while the first loop faces the periplasm.
| Original language | English |
|---|---|
| Pages (from-to) | 193-196 |
| Number of pages | 4 |
| Journal | FEBS Letters |
| Volume | 562 |
| Issue number | 1-3 |
| DOIs | |
| State | Published - 26 Mar 2004 |
Keywords
- Cysteine accessibility
- Drug resistance
- EmrE
- Membrane protein
- Smr