University Library
  • Login
A gateway to Melbourne's research publications
Minerva Access is the University's Institutional Repository. It aims to collect, preserve, and showcase the intellectual output of staff and students of the University of Melbourne for a global audience.
View Item 
  • Minerva Access
  • Medicine, Dentistry & Health Sciences
  • Melbourne Medical School
  • Biochemistry and Molecular Biology
  • Biochemistry and Molecular Biology - Research Publications
  • View Item
  • Minerva Access
  • Medicine, Dentistry & Health Sciences
  • Melbourne Medical School
  • Biochemistry and Molecular Biology
  • Biochemistry and Molecular Biology - Research Publications
  • View Item
JavaScript is disabled for your browser. Some features of this site may not work without it.

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

    Thumbnail
    Download
    Published version (4.862Mb)

    Citations
    Scopus
    Web of Science
    Altmetric
    20
    20
    Author
    Wahlgren, WY; Dunevall, E; North, RA; Paz, A; Scalise, M; Bisignano, P; Bengtsson-Palme, J; Goyal, P; Claesson, E; Caing-Carlsson, R; ...
    Date
    2018-05-01
    Source Title
    Nature Communications
    Publisher
    NATURE PUBLISHING GROUP
    University of Melbourne Author/s
    Dobson, Renwick
    Affiliation
    Biochemistry and Molecular Biology
    Metadata
    Show full item record
    Document Type
    Journal Article
    Citations
    Wahlgren, W. Y., Dunevall, E., North, R. A., Paz, A., Scalise, M., Bisignano, P., Bengtsson-Palme, J., Goyal, P., Claesson, E., Caing-Carlsson, R., Andersson, R., Beis, K., Nilsson, U. J., Farewell, A., Pochini, L., Indiveri, C., Grabe, M., Dobson, R. C. J., Abramson, J. ,... Friemann, R. (2018). Substrate-bound outward-open structure of a Na+-coupled sialic acid symporter reveals a new Na+ site. NATURE COMMUNICATIONS, 9 (1), https://doi.org/10.1038/s41467-018-04045-7.
    Access Status
    Open Access
    URI
    http://hdl.handle.net/11343/254999
    DOI
    10.1038/s41467-018-04045-7
    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.

    Export Reference in RIS Format     

    Endnote

    • Click on "Export Reference in RIS Format" and choose "open with... Endnote".

    Refworks

    • Click on "Export Reference in RIS Format". Login to Refworks, go to References => Import References


    Collections
    • Minerva Elements Records [45770]
    • Biochemistry and Molecular Biology - Research Publications [787]
    Minerva AccessDepositing Your Work (for University of Melbourne Staff and Students)NewsFAQs

    BrowseCommunities & CollectionsBy Issue DateAuthorsTitlesSubjectsThis CollectionBy Issue DateAuthorsTitlesSubjects
    My AccountLoginRegister
    StatisticsMost Popular ItemsStatistics by CountryMost Popular Authors