To the top

Page Manager: Webmaster
Last update: 9/11/2012 3:13 PM

Tell a friend about this page
Print version

Substrate-bound outward-o… - University of Gothenburg, Sweden Till startsida
Sitemap
To content Read more about how we use cookies on gu.se

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

Journal article
Authors Weixiao Yuan 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
Published in Nature Communications
Volume 9
Issue 1
ISSN 2041-1723
Publication year 2018
Published at Department of Chemistry and Molecular Biology
Centre for antibiotic resistance research, CARe
Institute of Biomedicine, Department of Infectious Medicine
Language en
Links dx.doi.org/10.1038/s41467-018-04045...
www.ncbi.nlm.nih.gov/entrez/query.f...
Subject categories Structural Biology, Biochemistry, Cell and molecular biology, Biophysics, Microbiology

Abstract

Many pathogenic bacteria utilise sialic acids as an energy source or use them as an external coating to evade immune detection. As such, bacteria that colonise sialylated environments deploy specific transporters to mediate import of scavenged sialic acids. Here, we report a substrate-bound 1.95 Å resolution structure and subsequent characterisation of SiaT, a sialic acid transporter from Proteus mirabilis. SiaT is a secondary active transporter of the sodium solute symporter (SSS) family, which use Na+ gradients to drive the uptake of extracellular substrates. SiaT adopts the LeuT-fold and is in an outward-open conformation in complex with the sialic acid N-acetylneuraminic acid and two Na+ ions. One Na+ binds to the conserved Na2 site, while the second Na+ binds to a new position, termed Na3, which is conserved in many SSS family members. Functional and molecular dynamics studies validate the substrate-binding site and demonstrate that both Na+ sites regulate N-acetylneuraminic acid transport.

Page Manager: Webmaster|Last update: 9/11/2012
Share:

The University of Gothenburg uses cookies to provide you with the best possible user experience. By continuing on this website, you approve of our use of cookies.  What are cookies?