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

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 and Rosmarie Friemann ()
Additional contact information
Weixiao Y. Wahlgren: University of Gothenburg
Elin Dunevall: University of Gothenburg
Rachel A. North: University of Gothenburg
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
Parveen Goyal: University of Gothenburg
Elin Claesson: University of Gothenburg
Rhawnie Caing-Carlsson: University of Gothenburg
Rebecka Andersson: University of Gothenburg
Konstantinos Beis: Imperial College London
Ulf J. Nilsson: Lund University
Anne Farewell: 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
Jeff Abramson: University of California
S. Ramaswamy: The Institute for Stem Cell Biology and Regenerative Medicine (InStem)
Rosmarie Friemann: University of Gothenburg

Nature Communications, 2018, vol. 9, issue 1, 1-14

Abstract: 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.

Date: 2018
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DOI: 10.1038/s41467-018-04045-7

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