Imperial College London
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DrKonstantinosBeis

Faculty of Natural Sciences, Department of Life Sciences

Reader in Membrane Protein Structural Biology
 
 
 
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Contact

 

konstantinos.beis Website

 
 
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Location

 

1-12Diamond Light Source LtdHarwell Science and Innovation Campus

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Summary

 

Publications

Citation

BibTex format

@article{Wahlgren:2018:10.1038/s41467-018-04045-7,
author = {Wahlgren, WY and Dunevall, E and North, RA and Paz, A and Scalise, M and Bisignano, P and Bengtsson-Palme, J and Goyal, P and Claesson, E and Caing-Carlsson, R and Andersson, R and Beis, K and Nilsson, UJ and Farewell, A and Pochini, L and Indiveri, C and Grabe, M and Dobson, RCJ and Abramson, J and Ramaswamy, S and Friemann, R},
doi = {10.1038/s41467-018-04045-7},
journal = {Nature Communications},
title = {Substrate-bound outward-open structure of a Na+-coupled sialic acid symporter reveals a new Na+ site},
url = {http://dx.doi.org/10.1038/s41467-018-04045-7},
volume = {9},
year = {2018}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - 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.
AU  - Wahlgren,WY
AU  - Dunevall,E
AU  - North,RA
AU  - Paz,A
AU  - Scalise,M
AU  - Bisignano,P
AU  - Bengtsson-Palme,J
AU  - Goyal,P
AU  - Claesson,E
AU  - Caing-Carlsson,R
AU  - Andersson,R
AU  - Beis,K
AU  - Nilsson,UJ
AU  - Farewell,A
AU  - Pochini,L
AU  - Indiveri,C
AU  - Grabe,M
AU  - Dobson,RCJ
AU  - Abramson,J
AU  - Ramaswamy,S
AU  - Friemann,R
DO  - 10.1038/s41467-018-04045-7
PY  - 2018///
SN  - 2041-1723
TI  - Substrate-bound outward-open structure of a Na+-coupled sialic acid symporter reveals a new Na+ site
T2  - Nature Communications
UR  - http://dx.doi.org/10.1038/s41467-018-04045-7
UR  - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000431119400005&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
UR  - http://hdl.handle.net/10044/1/59781
VL  - 9
ER  -
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