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==Structure of Arabidopsis thaliana sulfate transporter AtSULTR4;1==
<StructureSection load='7lhv' size='340' side='right'caption='[[7lhv]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LHV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LHV FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.75&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LBN:1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine'>LBN</scene>, <scene name='pdbligand=S1P:(2S,3R,4E)-2-AMINO-3-HYDROXYOCTADEC-4-EN-1-YL+DIHYDROGEN+PHOSPHATE'>S1P</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=7lhv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lhv OCA], [https://pdbe.org/7lhv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lhv RCSB], [https://www.ebi.ac.uk/pdbsum/7lhv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lhv ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Plant sulfate transporters (SULTR) mediate absorption and distribution of sulfate (SO4(2-)) and are essential for plant growth; however, our understanding of their structures and functions remains inadequate. Here we present the structure of a SULTR from Arabidopsis thaliana, AtSULTR4;1, in complex with SO4(2-) at an overall resolution of 2.8 A. AtSULTR4;1 forms a homodimer and has a structural fold typical of the SLC26 family of anion transporters. The bound SO4(2-) is coordinated by side-chain hydroxyls and backbone amides, and further stabilized electrostatically by the conserved Arg393 and two helix dipoles. Proton and SO4(2-) are co-transported by AtSULTR4;1 and a proton gradient significantly enhances SO4(2-) transport. Glu347, which is ~7 A from the bound SO4(2-), is required for H(+)-driven transport. The cytosolic STAS domain interacts with transmembrane domains, and deletion of the STAS domain or mutations to the interface compromises dimer formation and reduces SO4(2-) transport, suggesting a regulatory function of the STAS domain.

Structure and function of an Arabidopsis thaliana sulfate transporter.,Wang L, Chen K, Zhou M Nat Commun. 2021 Jul 22;12(1):4455. doi: 10.1038/s41467-021-24778-2. PMID:34294705<ref>PMID:34294705</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7lhv" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Chen K]]
[[Category: Wang L]]
[[Category: Zhou M]]