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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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Substrate-bound outward-open structure of a Na+-coupled sialic acid symporter reveals a new Na+ site
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Journal Article
Substrate-bound outward-open structure of a Na+-coupled sialic acid symporter reveals a new Na+ site
2018
Overview
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.
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.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 82/80
/ 82/83
/ Acids
/ Bacteria
/ Biofysik
/ Humanities and Social Sciences
/ Medicinska och farmaceutiska grundvetenskaper
/ Microbiology in the Medical Area
/ Mikrobiologi inom det medicinska området
/ N-Acetylneuraminic Acid - metabolism
/ Organic Anion Transporters - chemistry
/ Organic Anion Transporters - metabolism
/ Science
/ Sequence Homology, Amino Acid
/ Sodium
