View source for 5ys8


==2.8 angstrom crystal structure of Succinate-Acetate Permease from Citrobacter koseri==
<StructureSection load='5ys8' size='340' side='right'caption='[[5ys8]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ys8]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Citrobacter_koseri_ATCC_BAA-895 Citrobacter koseri ATCC BAA-895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YS8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YS8 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]] 2.798&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=78M:(2S)-2,3-DIHYDROXYPROPYL(7Z)-PENTADEC-7-ENOATE'>78M</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</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=5ys8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ys8 OCA], [https://pdbe.org/5ys8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ys8 RCSB], [https://www.ebi.ac.uk/pdbsum/5ys8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ys8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A8ALU5_CITK8 A8ALU5_CITK8] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Acetate is an important metabolite in metabolism and cell signaling. Succinate-Acetate Permease (SatP) superfamily proteins are known to be responsible for acetate transport across membranes, but the nature of this transport remains unknown. Here, we show that the SatP homolog from Citrobacter koseri (SatP_Ck) is an anion channel that can unidirectionally translocate acetate at rates of the order of ~10(7) ions/s. Crystal structures of SatP_Ck in complex with multiple acetates at 1.8 A reveal that the acetate pathway consists of four acetate-binding sites aligned in a single file that are interrupted by three hydrophobic constrictions. The bound acetates at the four sites are each orientated differently. The acetate at the cytoplasmic vestibule is partially dehydrated, whereas those in the main pore body are fully dehydrated. Aromatic residues within the substrate pathway may coordinate translocation of acetates via anion-pi interactions. SatP_Ck reveals a new type of selective anion channel and provides a structural and functional template for understanding organic anion transport.

Succinate-acetate permease from Citrobacter koseri is an anion channel that unidirectionally translocates acetate.,Qiu B, Xia B, Zhou Q, Lu Y, He M, Hasegawa K, Ma Z, Zhang F, Gu L, Mao Q, Wang F, Zhao S, Gao Z, Liao J Cell Res. 2018 Mar 27. pii: 10.1038/s41422-018-0032-8. doi:, 10.1038/s41422-018-0032-8. PMID:29588525<ref>PMID:29588525</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5ys8" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Citrobacter koseri ATCC BAA-895]]
[[Category: Large Structures]]
[[Category: Liao J]]
[[Category: Qiu B]]