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Article

The key residue for substrate transport (Glu14) in the EmrE dimer is asymmetric.

The Journal of biological chemistry - 8 Feb 2008

Lehner Ines, Basting Daniel, Meyer Bjoern, Haase Winfried, Manolikas Theofanis, Kaiser Christoph, Karas Michael, Glaubitz Clemens

Abstract excerpt

Transport proteins exhibiting broad substrate specificities are major determinants for the phenomenon of multidrug resistance. The Escherichia coli multidrug transporter EmrE, a 4-transmembrane, helical 12-kDa membrane protein, forms a functional dimer to transport a diverse array of aromatic, positively charged substrates in a proton/drug antiport fashion. Here, we report (13)C chemical shifts of the essential...

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PMID: 18042544
DOI: 10.1074/jbc.M707899200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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