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==1.8 angstrom crystal structure of Succinate-Acetate Permease from Citrobacter koseri==
==1.8 angstrom crystal structure of Succinate-Acetate Permease from Citrobacter koseri==
<StructureSection load='5ys3' size='340' side='right' caption='[[5ys3]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
<StructureSection load='5ys3' size='340' side='right'caption='[[5ys3]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5ys3]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Citk8 Citk8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YS3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YS3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5ys3]] 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=5YS3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YS3 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=78M:(2S)-2,3-DIHYDROXYPROPYL(7Z)-PENTADEC-7-ENOATE'>78M</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.823&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CKO_03375 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=290338 CITK8])</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>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ys3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ys3 OCA], [http://pdbe.org/5ys3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ys3 RCSB], [http://www.ebi.ac.uk/pdbsum/5ys3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ys3 ProSAT]</span></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=5ys3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ys3 OCA], [https://pdbe.org/5ys3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ys3 RCSB], [https://www.ebi.ac.uk/pdbsum/5ys3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ys3 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/A8ALU5_CITK8 A8ALU5_CITK8]
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 5ys3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Citk8]]
[[Category: Citrobacter koseri ATCC BAA-895]]
[[Category: Liao, J]]
[[Category: Large Structures]]
[[Category: Qiu, B]]
[[Category: Liao J]]
[[Category: Dehydration]]
[[Category: Qiu B]]
[[Category: Organic anion channel]]
[[Category: Rectifying]]
[[Category: Transport protein]]
[[Category: Unidirectional]]
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