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Analyzing conformational changes in the transport cycle of EmrE.

ABSTRACT: The small multidrug resistance transporters represent a unique model system for studying the mechanism of secondary active transport and membrane protein evolution. However, this seemingly simple protein has been highly controversial. Recent studies have provided experimental evidence that EmrE exists as an asymmetric dimer that exchanges between identical inward-facing and outward-facing states. Re-examination of the published literature in light of these findings fills in many details of the microscopic steps in the transport cycle. Future work will need to examine how the symmetry observed in vitro affects EmrE function in the asymmetric environment of its native Escherichia coli membrane.

SUBMITTER: Henzler-Wildman K

PROVIDER: S-EPMC3288627 | biostudies-literature | 2012 Feb

REPOSITORIES: biostudies-literature

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Analyzing conformational changes in the transport cycle of EmrE.

Henzler-Wildman Katherine K

Current opinion in structural biology 20111116 1

The small multidrug resistance transporters represent a unique model system for studying the mechanism of secondary active transport and membrane protein evolution. However, this seemingly simple protein has been highly controversial. Recent studies have provided experimental evidence that EmrE exists as an asymmetric dimer that exchanges between identical inward-facing and outward-facing states. Re-examination of the published literature in light of these findings fills in many details of the m ...[more]

PMID: 22100111

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