Outward open conformation of a Major Facilitator Superfamily multidrug/H+ antiporter provides insights into switching mechanism
The multidrug resistance transporter mediated efflux of antibiotics from the bacterial cytoplasm represents a major challenge to medicine. Here authors solve the X-ray crystallographic structure of the drug/H+ antiporter MdfA from Escherichia coli and shed light on the conformational switching mecha...
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Nature Portfolio
2018
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oai:doaj.org-article:9c31b685bee4442382a7b84e7402aa222021-12-02T15:33:56ZOutward open conformation of a Major Facilitator Superfamily multidrug/H+ antiporter provides insights into switching mechanism10.1038/s41467-018-06306-x2041-1723https://doaj.org/article/9c31b685bee4442382a7b84e7402aa222018-10-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-06306-xhttps://doaj.org/toc/2041-1723The multidrug resistance transporter mediated efflux of antibiotics from the bacterial cytoplasm represents a major challenge to medicine. Here authors solve the X-ray crystallographic structure of the drug/H+ antiporter MdfA from Escherichia coli and shed light on the conformational switching mechanism.Kumar NagarathinamYoshiko Nakada-NakuraChristoph ParthierTohru TeradaNarinobu JugeFrank JaeneckeKehong LiuYunhon HottaTakaaki MiyajiHiroshi OmoteSo IwataNorimichi NomuraMilton T. StubbsMikio TanabeNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-9 (2018) |
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DOAJ |
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DOAJ |
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EN |
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Science Q |
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Science Q Kumar Nagarathinam Yoshiko Nakada-Nakura Christoph Parthier Tohru Terada Narinobu Juge Frank Jaenecke Kehong Liu Yunhon Hotta Takaaki Miyaji Hiroshi Omote So Iwata Norimichi Nomura Milton T. Stubbs Mikio Tanabe Outward open conformation of a Major Facilitator Superfamily multidrug/H+ antiporter provides insights into switching mechanism |
| description |
The multidrug resistance transporter mediated efflux of antibiotics from the bacterial cytoplasm represents a major challenge to medicine. Here authors solve the X-ray crystallographic structure of the drug/H+ antiporter MdfA from Escherichia coli and shed light on the conformational switching mechanism. |
| format |
article |
| author |
Kumar Nagarathinam Yoshiko Nakada-Nakura Christoph Parthier Tohru Terada Narinobu Juge Frank Jaenecke Kehong Liu Yunhon Hotta Takaaki Miyaji Hiroshi Omote So Iwata Norimichi Nomura Milton T. Stubbs Mikio Tanabe |
| author_facet |
Kumar Nagarathinam Yoshiko Nakada-Nakura Christoph Parthier Tohru Terada Narinobu Juge Frank Jaenecke Kehong Liu Yunhon Hotta Takaaki Miyaji Hiroshi Omote So Iwata Norimichi Nomura Milton T. Stubbs Mikio Tanabe |
| author_sort |
Kumar Nagarathinam |
| title |
Outward open conformation of a Major Facilitator Superfamily multidrug/H+ antiporter provides insights into switching mechanism |
| title_short |
Outward open conformation of a Major Facilitator Superfamily multidrug/H+ antiporter provides insights into switching mechanism |
| title_full |
Outward open conformation of a Major Facilitator Superfamily multidrug/H+ antiporter provides insights into switching mechanism |
| title_fullStr |
Outward open conformation of a Major Facilitator Superfamily multidrug/H+ antiporter provides insights into switching mechanism |
| title_full_unstemmed |
Outward open conformation of a Major Facilitator Superfamily multidrug/H+ antiporter provides insights into switching mechanism |
| title_sort |
outward open conformation of a major facilitator superfamily multidrug/h+ antiporter provides insights into switching mechanism |
| publisher |
Nature Portfolio |
| publishDate |
2018 |
| url |
https://doaj.org/article/9c31b685bee4442382a7b84e7402aa22 |
| work_keys_str_mv |
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| _version_ |
1718386979550265344 |