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 |
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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