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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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  • Weixiao Y. Wahlgren

    (University of Gothenburg
    Centre for Antibiotic Resistance Research (CARe) at University of Gothenburg
    Imperial College London
    Harwell Science and Innovation Campus)

  • Elin Dunevall

    (University of Gothenburg)

  • Rachel A. North

    (University of Gothenburg
    University of Canterbury)

  • Aviv Paz

    (University of California)

  • Mariafrancesca Scalise

    (University of Calabria)

  • Paola Bisignano

    (University of California)

  • Johan Bengtsson-Palme

    (Centre for Antibiotic Resistance Research (CARe) at University of Gothenburg
    University of Gothenburg)

  • Parveen Goyal

    (University of Gothenburg
    Centre for Antibiotic Resistance Research (CARe) at University of Gothenburg)

  • Elin Claesson

    (University of Gothenburg)

  • Rhawnie Caing-Carlsson

    (University of Gothenburg)

  • Rebecka Andersson

    (University of Gothenburg)

  • Konstantinos Beis

    (Imperial College London
    Harwell Science and Innovation Campus
    Research Complex at Harwell)

  • Ulf J. Nilsson

    (Lund University)

  • Anne Farewell

    (University of Gothenburg
    Centre for Antibiotic Resistance Research (CARe) at University of Gothenburg)

  • Lorena Pochini

    (University of Calabria)

  • Cesare Indiveri

    (University of Calabria)

  • Michael Grabe

    (University of California)

  • Renwick C. J. Dobson

    (University of Canterbury
    University of Melbourne)

  • Jeff Abramson

    (University of California
    The Institute for Stem Cell Biology and Regenerative Medicine (InStem))

  • S. Ramaswamy

    (The Institute for Stem Cell Biology and Regenerative Medicine (InStem))

  • Rosmarie Friemann

    (University of Gothenburg
    Centre for Antibiotic Resistance Research (CARe) at University of Gothenburg
    School of Medicine Stanford University)

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.

Suggested Citation

  • 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 A, 2018. "Substrate-bound outward-open structure of a Na+-coupled sialic acid symporter reveals a new Na+ site," Nature Communications, Nature, vol. 9(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-04045-7
    DOI: 10.1038/s41467-018-04045-7
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    Cited by:

    1. Farha Khan & Matthias Elgeti & Samuel Grandfield & Aviv Paz & Fiona B. Naughton & Frank V. Marcoline & Thorsten Althoff & Natalia Ermolova & Ernest M. Wright & Wayne L. Hubbell & Michael Grabe & Jeff , 2023. "Membrane potential accelerates sugar uptake by stabilizing the outward facing conformation of the Na/glucose symporter vSGLT," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    2. Yange Niu & Wenhao Cui & Rui Liu & Sanshan Wang & Han Ke & Xiaoguang Lei & Lei Chen, 2022. "Structural mechanism of SGLT1 inhibitors," Nature Communications, Nature, vol. 13(1), pages 1-10, December.
    3. James S. Davies & Michael J. Currie & Rachel A. North & Mariafrancesca Scalise & Joshua D. Wright & Jack M. Copping & Daniela M. Remus & Ashutosh Gulati & Dustin R. Morado & Sam A. Jamieson & Michael , 2023. "Structure and mechanism of a tripartite ATP-independent periplasmic TRAP transporter," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    4. Martin F. Peter & Jan A. Ruland & Peer Depping & Niels Schneberger & Emmanuele Severi & Jonas Moecking & Karl Gatterdam & Sarah Tindall & Alexandre Durand & Veronika Heinz & Jan Peter Siebrasse & Paul, 2022. "Structural and mechanistic analysis of a tripartite ATP-independent periplasmic TRAP transporter," Nature Communications, Nature, vol. 13(1), pages 1-15, December.

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