Substrate-bound outward-open structure of a Na+-coupled sialic acid symporter reveals a new Na+ site

Sialic acid transporters (SiaT) are required for sialic acid uptake in a number of human pathogens and are of interest as targets for antimicrobial drug development. Here the authors present the substrate bound SiaT structure from the uropathogen Proteus mirabilis and provide insights into the mecha...

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Autores principales:	Weixiao Y. Wahlgren, Elin Dunevall, Rachel A. North, Aviv Paz, Mariafrancesca Scalise, Paola Bisignano, Johan Bengtsson-Palme, Parveen Goyal, Elin Claesson, Rhawnie Caing-Carlsson, Rebecka Andersson, Konstantinos Beis, Ulf J. Nilsson, Anne Farewell, Lorena Pochini, Cesare Indiveri, Michael Grabe, Renwick C. J. Dobson, Jeff Abramson, S. Ramaswamy, Rosmarie Friemann
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/64411a096c2a4afbaca431c776617538
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spelling	oai:doaj.org-article:64411a096c2a4afbaca431c7766175382021-12-02T14:40:43ZSubstrate-bound outward-open structure of a Na+-coupled sialic acid symporter reveals a new Na+ site10.1038/s41467-018-04045-72041-1723https://doaj.org/article/64411a096c2a4afbaca431c7766175382018-05-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-04045-7https://doaj.org/toc/2041-1723Sialic acid transporters (SiaT) are required for sialic acid uptake in a number of human pathogens and are of interest as targets for antimicrobial drug development. Here the authors present the substrate bound SiaT structure from the uropathogen Proteus mirabilis and provide insights into the mechanism of sialic acid transport.Weixiao Y. WahlgrenElin DunevallRachel A. NorthAviv PazMariafrancesca ScalisePaola BisignanoJohan Bengtsson-PalmeParveen GoyalElin ClaessonRhawnie Caing-CarlssonRebecka AnderssonKonstantinos BeisUlf J. NilssonAnne FarewellLorena PochiniCesare IndiveriMichael GrabeRenwick C. J. DobsonJeff AbramsonS. RamaswamyRosmarie FriemannNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-14 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Weixiao Y. Wahlgren Elin Dunevall Rachel A. North Aviv Paz Mariafrancesca Scalise Paola Bisignano Johan Bengtsson-Palme Parveen Goyal Elin Claesson Rhawnie Caing-Carlsson Rebecka Andersson Konstantinos Beis Ulf J. Nilsson Anne Farewell Lorena Pochini Cesare Indiveri Michael Grabe Renwick C. J. Dobson Jeff Abramson S. Ramaswamy Rosmarie Friemann Substrate-bound outward-open structure of a Na+-coupled sialic acid symporter reveals a new Na+ site
description	Sialic acid transporters (SiaT) are required for sialic acid uptake in a number of human pathogens and are of interest as targets for antimicrobial drug development. Here the authors present the substrate bound SiaT structure from the uropathogen Proteus mirabilis and provide insights into the mechanism of sialic acid transport.
format	article
author	Weixiao Y. Wahlgren Elin Dunevall Rachel A. North Aviv Paz Mariafrancesca Scalise Paola Bisignano Johan Bengtsson-Palme Parveen Goyal Elin Claesson Rhawnie Caing-Carlsson Rebecka Andersson Konstantinos Beis Ulf J. Nilsson Anne Farewell Lorena Pochini Cesare Indiveri Michael Grabe Renwick C. J. Dobson Jeff Abramson S. Ramaswamy Rosmarie Friemann
author_facet	Weixiao Y. Wahlgren Elin Dunevall Rachel A. North Aviv Paz Mariafrancesca Scalise Paola Bisignano Johan Bengtsson-Palme Parveen Goyal Elin Claesson Rhawnie Caing-Carlsson Rebecka Andersson Konstantinos Beis Ulf J. Nilsson Anne Farewell Lorena Pochini Cesare Indiveri Michael Grabe Renwick C. J. Dobson Jeff Abramson S. Ramaswamy Rosmarie Friemann
author_sort	Weixiao Y. Wahlgren
title	Substrate-bound outward-open structure of a Na+-coupled sialic acid symporter reveals a new Na+ site
title_short	Substrate-bound outward-open structure of a Na+-coupled sialic acid symporter reveals a new Na+ site
title_full	Substrate-bound outward-open structure of a Na+-coupled sialic acid symporter reveals a new Na+ site
title_fullStr	Substrate-bound outward-open structure of a Na+-coupled sialic acid symporter reveals a new Na+ site
title_full_unstemmed	Substrate-bound outward-open structure of a Na+-coupled sialic acid symporter reveals a new Na+ site
title_sort	substrate-bound outward-open structure of a na+-coupled sialic acid symporter reveals a new na+ site
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/64411a096c2a4afbaca431c776617538
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Substrate-bound outward-open structure of a Na+-coupled sialic acid symporter reveals a new Na+ site

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