7ynk: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7ynk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YNK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YNK FirstGlance]. <br> | <table><tr><td colspan='2'>[[7ynk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YNK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YNK FirstGlance]. <br> | ||
</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=7ynk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ynk OCA], [https://pdbe.org/7ynk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ynk RCSB], [https://www.ebi.ac.uk/pdbsum/7ynk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ynk ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.48Å</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=7ynk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ynk OCA], [https://pdbe.org/7ynk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ynk RCSB], [https://www.ebi.ac.uk/pdbsum/7ynk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ynk ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Disease == | == Disease == | ||
[https://www.uniprot.org/uniprot/SC5A2_HUMAN SC5A2_HUMAN] Familial renal glucosuria. The disease is caused by variants affecting the gene represented in this entry. | [https://www.uniprot.org/uniprot/SC5A2_HUMAN SC5A2_HUMAN] Familial renal glucosuria. The disease is caused by variants affecting the gene represented in this entry. | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/SC5A2_HUMAN SC5A2_HUMAN] Electrogenic Na(+)-coupled sugar | [https://www.uniprot.org/uniprot/SC5A2_HUMAN SC5A2_HUMAN] Electrogenic Na(+)-coupled sugar symporter that actively transports D-glucose at the plasma membrane, with a Na(+) to sugar coupling ratio of 1:1. Transporter activity is driven by a transmembrane Na(+) electrochemical gradient set by the Na(+)/K(+) pump (PubMed:20980548, PubMed:28592437, PubMed:34880493). Has a primary role in D-glucose reabsorption from glomerular filtrate across the brush border of the early proximal tubules of the kidney (By similarity).[UniProtKB:Q923I7]<ref>PMID:20980548</ref> <ref>PMID:28592437</ref> <ref>PMID:34880493</ref> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Sodium-Glucose Cotransporters (SGLT) mediate the uphill uptake of extracellular sugars and play fundamental roles in sugar metabolism. Although their structures in inward-open and outward-open conformations are emerging from structural studies, the trajectory of how SGLTs transit from the outward-facing to the inward-facing conformation remains unknown. Here, we present the cryo-EM structures of human SGLT1 and SGLT2 in the substrate-bound state. Both structures show an occluded conformation, with not only the extracellular gate but also the intracellular gate tightly sealed. The sugar substrate are caged inside a cavity surrounded by TM1, TM2, TM3, TM6, TM7, and TM10. Further structural analysis reveals the conformational changes associated with the binding and release of substrates. These structures fill a gap in our understanding of the structural mechanisms of SGLT transporters. | |||
Structures of human SGLT in the occluded state reveal conformational changes during sugar transport.,Cui W, Niu Y, Sun Z, Liu R, Chen L Nat Commun. 2023 May 22;14(1):2920. doi: 10.1038/s41467-023-38720-1. PMID:37217492<ref>PMID:37217492</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7ynk" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Sodium/glucose cotransporter 3D structures|Sodium/glucose cotransporter 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Latest revision as of 14:50, 30 October 2024
Structure of human SGLT2-MAP17 complex in the apo state in the inward-facing conformationStructure of human SGLT2-MAP17 complex in the apo state in the inward-facing conformation
Structural highlights
DiseaseSC5A2_HUMAN Familial renal glucosuria. The disease is caused by variants affecting the gene represented in this entry. FunctionSC5A2_HUMAN Electrogenic Na(+)-coupled sugar symporter that actively transports D-glucose at the plasma membrane, with a Na(+) to sugar coupling ratio of 1:1. Transporter activity is driven by a transmembrane Na(+) electrochemical gradient set by the Na(+)/K(+) pump (PubMed:20980548, PubMed:28592437, PubMed:34880493). Has a primary role in D-glucose reabsorption from glomerular filtrate across the brush border of the early proximal tubules of the kidney (By similarity).[UniProtKB:Q923I7][1] [2] [3] Publication Abstract from PubMedSodium-Glucose Cotransporters (SGLT) mediate the uphill uptake of extracellular sugars and play fundamental roles in sugar metabolism. Although their structures in inward-open and outward-open conformations are emerging from structural studies, the trajectory of how SGLTs transit from the outward-facing to the inward-facing conformation remains unknown. Here, we present the cryo-EM structures of human SGLT1 and SGLT2 in the substrate-bound state. Both structures show an occluded conformation, with not only the extracellular gate but also the intracellular gate tightly sealed. The sugar substrate are caged inside a cavity surrounded by TM1, TM2, TM3, TM6, TM7, and TM10. Further structural analysis reveals the conformational changes associated with the binding and release of substrates. These structures fill a gap in our understanding of the structural mechanisms of SGLT transporters. Structures of human SGLT in the occluded state reveal conformational changes during sugar transport.,Cui W, Niu Y, Sun Z, Liu R, Chen L Nat Commun. 2023 May 22;14(1):2920. doi: 10.1038/s41467-023-38720-1. PMID:37217492[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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