6d79

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<StructureSection load='6d79' size='340' side='right' caption='[[6d79]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
<StructureSection load='6d79' size='340' side='right' caption='[[6d79]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6d79]] is a 2 chain structure. 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>
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<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>
</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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3tx3|3tx3]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3tx3|3tx3]]</td></tr>
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<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'>[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>
<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 ==
== 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]
[[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]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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<ref>PMID:29792261</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6d79" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Pseudomonas fragi a22]]
[[Category: Banerjee, S]]
[[Category: Banerjee, S]]
[[Category: Clarke, O B]]
[[Category: Clarke, O B]]

Revision as of 06:21, 6 June 2018

Structure of CysZ, a sulfate permease from Pseudomonas Fragi

6d79, resolution 3.50Å

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