View source for 5nva


==Substrate-bound outward-open state of a Na+-coupled sialic acid symporter reveals a novel Na+-site==
<StructureSection load='5nva' size='340' side='right'caption='[[5nva]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5nva]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Proteus_mirabilis_HI4320 Proteus mirabilis HI4320]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NVA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NVA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.26&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SLB:5-N-ACETYL-BETA-D-NEURAMINIC+ACID'>SLB</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5nva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nva OCA], [https://pdbe.org/5nva PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nva RCSB], [https://www.ebi.ac.uk/pdbsum/5nva PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nva ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B4EZY7_PROMH B4EZY7_PROMH] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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 A 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.

Substrate-bound outward-open structure of a Na(+)-coupled sialic acid symporter reveals a new Na(+) site.,Wahlgren WY, Dunevall E, North RA, Paz A, Scalise M, Bisignano P, Bengtsson-Palme J, Goyal P, Claesson E, Caing-Carlsson R, Andersson R, Beis K, Nilsson UJ, Farewell A, Pochini L, Indiveri C, Grabe M, Dobson RCJ, Abramson J, Ramaswamy S, Friemann R Nat Commun. 2018 May 1;9(1):1753. doi: 10.1038/s41467-018-04045-7. PMID:29717135<ref>PMID:29717135</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5nva" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Proteus mirabilis HI4320]]
[[Category: Abramson J]]
[[Category: Dobson R]]
[[Category: Dunevall E]]
[[Category: Friemann R]]
[[Category: Goyal P]]
[[Category: Grabe M]]
[[Category: North RA]]
[[Category: Ramaswamy S]]
[[Category: Wahlgren WY]]