Journal
FEBS LETTERS
Volume 562, Issue 1-3, Pages 193-196Publisher
WILEY
DOI: 10.1016/S0014-5793(04)00240-6
Keywords
EmrE; membrane protein; drug resistance; Smr; cysteine accessibility
Funding
- NINDS NIH HHS [NS16708] Funding Source: Medline
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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. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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