View source for 5zug


==Structure of the bacterial acetate channel SatP==
<StructureSection load='5zug' size='340' side='right'caption='[[5zug]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5zug]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZUG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZUG 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]] 2.802&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BNG:B-NONYLGLUCOSIDE'>BNG</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=5zug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zug OCA], [https://pdbe.org/5zug PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zug RCSB], [https://www.ebi.ac.uk/pdbsum/5zug PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zug ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SATP_ECOLI SATP_ECOLI] Uptake of acetate and succinate. Transport is energetically dependent on the protonmotive force.<ref>PMID:23844911</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Acetate is found ubiquitously in the natural environment and can be used as an exogenous carbon source by bacteria, fungi, and mammalian cells. A representative member of the acetate uptake transporter (AceTr) family named SatP (also yaaH) has been preliminarily identified as a succinate-acetate/proton symporter in Escherichia coli However, the molecular mechanism of acetate uptake by SatP still remains elusive. Here, we report the crystal structure of SatP from E. coli at 2.8 A resolution, determined with a molecular replacement approach using a previously developed predicted model algorithm, which revealed a hexameric UreI-like channel structure. Structural analysis identified six transmembrane (TM) helices surrounding the central channel pore in each protomer and three conserved hydrophobic residues, FLY, located in the middle of the TM region for pore constriction. According to single-channel conductance recordings, performed with purified SatP reconstituted into lipid bilayer, three conserved polar residues in the TM1 facing to the periplasmic side are closely associated with acetate translocation activity. These analyses provide critical insights into the mechanism of acetate translocation in bacteria and a first glimpse of a structure of an AceTr family transporter.

Crystal structure of the bacterial acetate transporter SatP reveals that it forms a hexameric channel.,Sun P, Li J, Zhang X, Guan Z, Xiao Q, Zhao C, Song M, Zhou Y, Mou L, Ke M, Guo L, Geng J, Deng D J Biol Chem. 2018 Dec 14;293(50):19492-19500. doi: 10.1074/jbc.RA118.003876. Epub, 2018 Oct 17. PMID:30333234<ref>PMID:30333234</ref>

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

==See Also==
*[[Symporter 3D structures|Symporter 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Deng D]]
[[Category: Guan ZY]]
[[Category: Li JL]]
[[Category: Sun PC]]
[[Category: Xiao QJ]]