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Outward open conformation of a Major Facilitator Superfamily multidrug/H+ antiporter provides insigh...

Outward open conformation of a Major Facilitator Superfamily multidrug/H+ antiporter provides insigh...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_9c31b685bee4442382a7b84e7402aa22

Outward open conformation of a Major Facilitator Superfamily multidrug/H+ antiporter provides insights into switching mechanism

About this item

Full title

Outward open conformation of a Major Facilitator Superfamily multidrug/H+ antiporter provides insights into switching mechanism

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2018-10, Vol.9 (1), p.4005-9, Article 4005

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Multidrug resistance (MDR) poses a major challenge to medicine. A principle cause of MDR is through active efflux by MDR transporters situated in the bacterial membrane. Here we present the crystal structure of the major facilitator superfamily (MFS) drug/H
+
antiporter MdfA from
Escherichia coli
in an outward open conformation. Compari...

Alternative Titles

Full title

Outward open conformation of a Major Facilitator Superfamily multidrug/H+ antiporter provides insights into switching mechanism

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_9c31b685bee4442382a7b84e7402aa22

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_9c31b685bee4442382a7b84e7402aa22

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/s41467-018-06306-x

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