View source for 5xat


==Structural insights into the elevator-like mechanism of the sodium/citrate symporter CitS==
<StructureSection load='5xat' size='340' side='right'caption='[[5xat]], [[Resolution|resolution]] 3.76&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5xat]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XAT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XAT 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]] 3.76&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=5xat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xat OCA], [https://pdbe.org/5xat PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xat RCSB], [https://www.ebi.ac.uk/pdbsum/5xat PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xat ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CITN_KLEPN CITN_KLEPN] Uptake of citrate across the boundary membrane with the concomitant uptake of a sodium ion (symport system).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The sodium-dependent citrate transporter of Klebsiella pneumoniae (KpCitS) belongs to the 2-hydroxycarboxylate transporter (2-HCT) family and allows the cell to use citrate as sole carbon and energy source in anaerobic conditions. Here we present crystal structures of KpCitS in citrate-bound outward-facing, citrate-bound asymmetric, and citrate-free inward-facing state. The structures reveal that the KpCitS dimerization domain remains stationary throughout the transport cycle due to a hydrogen bond network as well as extensive hydrophobic interactions. In contrast, its transport domain undergoes a ~35 degrees rigid-body rotation and a ~17 A translocation perpendicular to the membrane to expose the substrate-binding site alternately to either side of the membrane. Furthermore, homology models of two other 2-HCT proteins based on the KpCitS structure offer structural insights into their differences in substrate specificity at a molecular level. On the basis of our results and previous biochemical data, we propose that the activity of the 2-HCT CitS involves an elevator-like movement in which the transport domain itself traverses the lipid bilayer, carrying the substrate into the cell in a sodium-dependent manner.

Structural insights into the elevator-like mechanism of the sodium/citrate symporter CitS.,Kim JW, Kim S, Kim S, Lee H, Lee JO, Jin MS Sci Rep. 2017 May 31;7(1):2548. doi: 10.1038/s41598-017-02794-x. PMID:28566738<ref>PMID:28566738</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5xat" style="background-color:#fffaf0;"></div>

==See Also==
*[[Symporter 3D structures|Symporter 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Klebsiella pneumoniae]]
[[Category: Large Structures]]
[[Category: Jin MS]]
[[Category: Kim JW]]
[[Category: Kim S]]
[[Category: Lee H]]
[[Category: Lee J-O]]