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| | <StructureSection load='6d79' size='340' side='right'caption='[[6d79]], [[Resolution|resolution]] 3.50Å' scene=''> | | <StructureSection load='6d79' size='340' side='right'caption='[[6d79]], [[Resolution|resolution]] 3.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6d79]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_fragi_a22 Pseudomonas fragi a22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6D79 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6D79 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6d79]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_fragi_A22 Pseudomonas fragi A22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6D79 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6D79 FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 3.501Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3tx3|3tx3]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cysZ, AV641_18770 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1134475 Pseudomonas fragi A22])</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=6d79 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d79 OCA], [https://pdbe.org/6d79 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6d79 RCSB], [https://www.ebi.ac.uk/pdbsum/6d79 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6d79 ProSAT]</span></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=6d79 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d79 OCA], [http://pdbe.org/6d79 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6d79 RCSB], [http://www.ebi.ac.uk/pdbsum/6d79 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6d79 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | == Function == | |
| - | [[http://www.uniprot.org/uniprot/A0A0X8F058_PSEFR A0A0X8F058_PSEFR]] High affinity, high specificity proton-dependent sulfate transporter, which mediates sulfate uptake. Provides the sulfur source for the cysteine synthesis pathway.[HAMAP-Rule:MF_00468][SAAS:SAAS00541081] | |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pseudomonas fragi a22]] | + | [[Category: Pseudomonas fragi A22]] |
| - | [[Category: Banerjee, S]] | + | [[Category: Banerjee S]] |
| - | [[Category: Clarke, O B]] | + | [[Category: Clarke OB]] |
| - | [[Category: Hendrickson, W A]] | + | [[Category: Hendrickson WA]] |
| - | [[Category: Liu, Q]] | + | [[Category: Liu Q]] |
| - | [[Category: Mancia, F]] | + | [[Category: Mancia F]] |
| - | [[Category: Rajashankar, K R]] | + | [[Category: Rajashankar KR]] |
| - | [[Category: Sanghai, Z A]] | + | [[Category: Sanghai ZA]] |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Prokaryotic cysteine biosynthesis]]
| + | |
| - | [[Category: Sulfate translocation]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Publication Abstract from PubMed
Sulfur, most abundantly found in the environment as sulfate (SO4(2-)), is an essential element in metabolites required by all living cells, including amino acids, co-factors and vitamins. However, current understanding of the cellular delivery of SO4(2-) at the molecular level is limited. CysZ has been described as a SO4(2-) permease, but its sequence family is without known structural precedent. Based on crystallographic structure information, SO4(2-) binding and flux experiments, we provide insight into the molecular mechanism of CysZ-mediated translocation of SO4(2-) across membranes. CysZ structures from three different bacterial species display a hitherto unknown fold and have subunits organized with inverted transmembrane topology. CysZ from Pseudomonas denitrificans assembles as a trimer of antiparallel dimers and the CysZ structures from two other species recapitulate dimers from this assembly. Mutational studies highlight the functional relevance of conserved CysZ residues.
Structure-based analysis of CysZ-mediated cellular uptake of sulfate.,Assur Sanghai Z, Liu Q, Clarke OB, Belcher-Dufrisne M, Wiriyasermkul P, Giese MH, Leal-Pinto E, Kloss B, Tabuso S, Love J, Punta M, Banerjee S, Rajashankar KR, Rost B, Logothetis D, Quick M, Hendrickson WA, Mancia F Elife. 2018 May 24;7. pii: 27829. doi: 10.7554/eLife.27829. PMID:29792261[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Assur Sanghai Z, Liu Q, Clarke OB, Belcher-Dufrisne M, Wiriyasermkul P, Giese MH, Leal-Pinto E, Kloss B, Tabuso S, Love J, Punta M, Banerjee S, Rajashankar KR, Rost B, Logothetis D, Quick M, Hendrickson WA, Mancia F. Structure-based analysis of CysZ-mediated cellular uptake of sulfate. Elife. 2018 May 24;7. pii: 27829. doi: 10.7554/eLife.27829. PMID:29792261 doi:http://dx.doi.org/10.7554/eLife.27829
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