Nature Communications (May 2018)
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,
- Rosmarie Friemann
Affiliations
- Weixiao Y. Wahlgren
- Department of Chemistry and Molecular Biology, University of Gothenburg
- Elin Dunevall
- Department of Chemistry and Molecular Biology, University of Gothenburg
- Rachel A. North
- Department of Chemistry and Molecular Biology, University of Gothenburg
- Aviv Paz
- Department of Physiology, David Geffen School of Medicine, University of California
- Mariafrancesca Scalise
- Department DiBEST (Biologia, Ecologia, Scienze della Terra) Unit of Biochemistry and Molecular Biotechnology, University of Calabria
- Paola Bisignano
- Cardiovascular Research Institute, Department of Pharmaceutical Chemistry, University of California
- Johan Bengtsson-Palme
- Centre for Antibiotic Resistance Research (CARe) at University of Gothenburg
- Parveen Goyal
- Department of Chemistry and Molecular Biology, University of Gothenburg
- Elin Claesson
- Department of Chemistry and Molecular Biology, University of Gothenburg
- Rhawnie Caing-Carlsson
- Department of Chemistry and Molecular Biology, University of Gothenburg
- Rebecka Andersson
- Department of Chemistry and Molecular Biology, University of Gothenburg
- Konstantinos Beis
- Department of Life Sciences, Imperial College London
- Ulf J. Nilsson
- Centre for Analysis and Synthesis, Department of Chemistry, Lund University
- Anne Farewell
- Department of Chemistry and Molecular Biology, University of Gothenburg
- Lorena Pochini
- Department DiBEST (Biologia, Ecologia, Scienze della Terra) Unit of Biochemistry and Molecular Biotechnology, University of Calabria
- Cesare Indiveri
- Department DiBEST (Biologia, Ecologia, Scienze della Terra) Unit of Biochemistry and Molecular Biotechnology, University of Calabria
- Michael Grabe
- Cardiovascular Research Institute, Department of Pharmaceutical Chemistry, University of California
- Renwick C. J. Dobson
- Biomolecular Interaction Centre and School of Biological Sciences, University of Canterbury
- Jeff Abramson
- Department of Physiology, David Geffen School of Medicine, University of California
- S. Ramaswamy
- The Institute for Stem Cell Biology and Regenerative Medicine (InStem)
- Rosmarie Friemann
- Department of Chemistry and Molecular Biology, University of Gothenburg
- DOI
- https://doi.org/10.1038/s41467-018-04045-7
- Journal volume & issue
-
Vol. 9,
no. 1
pp. 1 – 14
Abstract
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.
