View source for 5xls


==Crystal structure of UraA in occluded conformation==
<StructureSection load='5xls' size='340' side='right'caption='[[5xls]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5xls]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XLS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XLS 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]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=URA:URACIL'>URA</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=5xls FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xls OCA], [https://pdbe.org/5xls PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xls RCSB], [https://www.ebi.ac.uk/pdbsum/5xls PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xls ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/URAA_ECO57 URAA_ECO57] Transport of uracil in the cell.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Escherichia coli uracil:proton symporter UraA is a prototypical member of the nucleobase/ascorbate transporter (NAT) or nucleobase/cation symporter 2 (NCS2) family, which corresponds to the human solute carrier family SLC23. UraA consists of 14 transmembrane segments (TMs) that are organized into two distinct domains, the core domain and the gate domain, a structural fold that is also shared by the SLC4 and SLC26 transporters. Here we present the crystal structure of UraA bound to uracil in an occluded state at 2.5 A resolution. Structural comparison with the previously reported inward-open UraA reveals pronounced relative motions between the core domain and the gate domain as well as intra-domain rearrangement of the gate domain. The occluded UraA forms a dimer in the structure wherein the gate domains are sandwiched by two core domains. In vitro and in vivo biochemical characterizations show that UraA is at equilibrium between dimer and monomer in all tested detergent micelles, while dimer formation is necessary for the transport activity. Structural comparison between the dimeric UraA and the recently reported inward-facing dimeric UapA provides important insight into the transport mechanism of SLC23 transporters.

Dimeric structure of the uracil:proton symporter UraA provides mechanistic insights into the SLC4/23/26 transporters.,Yu X, Yang G, Yan C, Baylon JL, Jiang J, Fan H, Lu G, Hasegawa K, Okumura H, Wang T, Tajkhorshid E, Li S, Yan N Cell Res. 2017 Aug;27(8):1020-1033. doi: 10.1038/cr.2017.83. Epub 2017 Jun 16. PMID:28621327<ref>PMID:28621327</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5xls" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli O157:H7]]
[[Category: Large Structures]]
[[Category: Yan CY]]
[[Category: Yan N]]
[[Category: Yang GH]]
[[Category: Yu XZ]]