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High-pH structure of EmrE reveals the mechanism of proton-coupled substrate transport

High-pH structure of EmrE reveals the mechanism of proton-coupled substrate transport

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_a6ff24e0a3844b76b2840e90afda18df

High-pH structure of EmrE reveals the mechanism of proton-coupled substrate transport

About this item

Full title

High-pH structure of EmrE reveals the mechanism of proton-coupled substrate transport

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2022-02, Vol.13 (1), p.991-991, Article 991

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

The homo-dimeric bacterial membrane protein EmrE effluxes polyaromatic cationic substrates in a proton-coupled manner to cause multidrug resistance. We recently determined the structure of substrate-bound EmrE in phospholipid bilayers by measuring hundreds of protein-ligand H
N
–F distances for a fluorinated substrate, 4-fluoro-tetraphenylpho...

Alternative Titles

Full title

High-pH structure of EmrE reveals the mechanism of proton-coupled substrate transport

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_a6ff24e0a3844b76b2840e90afda18df

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_a6ff24e0a3844b76b2840e90afda18df

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/s41467-022-28556-6

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