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| | <StructureSection load='5uhs' size='340' side='right'caption='[[5uhs]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='5uhs' size='340' side='right'caption='[[5uhs]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5uhs]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lepbp Lepbp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UHS OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5UHS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5uhs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Leptospira_biflexa_serovar_Patoc_strain_'Patoc_1_(Paris)' Leptospira biflexa serovar Patoc strain 'Patoc 1 (Paris)']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UHS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=MVC:MONOVACCENIN'>MVC</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]] 2.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5uhq|5uhq]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=MVC:MONOVACCENIN'>MVC</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LEPBI_I1613 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=456481 LEPBP])</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=5uhs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uhs OCA], [https://pdbe.org/5uhs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5uhs RCSB], [https://www.ebi.ac.uk/pdbsum/5uhs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5uhs ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5uhs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uhs OCA], [http://pdbe.org/5uhs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uhs RCSB], [http://www.ebi.ac.uk/pdbsum/5uhs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uhs ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SWEET_LEPBP SWEET_LEPBP]] The homodimer mediates transmembrane sugar transport down a concentration gradient. Transport is probably effected by rocking-type movements, where a cargo-binding cavity opens first on one and then on the other side of the membrane.<ref>PMID:25186729</ref> | + | [https://www.uniprot.org/uniprot/SWEET_LEPBP SWEET_LEPBP] The homodimer mediates transmembrane sugar transport down a concentration gradient. Transport is probably effected by rocking-type movements, where a cargo-binding cavity opens first on one and then on the other side of the membrane.<ref>PMID:25186729</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5uhs" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5uhs" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[ABC transporter 3D structures|ABC transporter 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lepbp]]
| + | [[Category: Fastman NM]] |
| - | [[Category: Fastman, N M]] | + | [[Category: Feng L]] |
| - | [[Category: Feng, L]] | + | |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: Semisweet]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| - | [[Category: Transporter]]
| + | |
| Structural highlights
Function
SWEET_LEPBP The homodimer mediates transmembrane sugar transport down a concentration gradient. Transport is probably effected by rocking-type movements, where a cargo-binding cavity opens first on one and then on the other side of the membrane.[1]
Publication Abstract from PubMed
Transporters shuttle molecules across cell membranes by alternating among distinct conformational states. Fundamental questions remain about how transporters transition between states and how such structural rearrangements regulate substrate translocation. Here, we capture the translocation process by crystallography and unguided molecular dynamics simulations, providing an atomic-level description of alternating access transport. Simulations of a SWEET-family transporter initiated from an outward-open, glucose-bound structure reported here spontaneously adopt occluded and inward-open conformations. Strikingly, these conformations match crystal structures, including our inward-open structure. Mutagenesis experiments further validate simulation predictions. Our results reveal that state transitions are driven by favorable interactions formed upon closure of extracellular and intracellular "gates" and by an unfavorable transmembrane helix configuration when both gates are closed. This mechanism leads to tight allosteric coupling between gates, preventing them from opening simultaneously. Interestingly, the substrate appears to take a "free ride" across the membrane without causing major structural rearrangements in the transporter.
Mechanism of Substrate Translocation in an Alternating Access Transporter.,Latorraca NR, Fastman NM, Venkatakrishnan AJ, Frommer WB, Dror RO, Feng L Cell. 2017 Mar 23;169(1):96-107.e12. doi: 10.1016/j.cell.2017.03.010. PMID:28340354[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Xu Y, Tao Y, Cheung LS, Fan C, Chen LQ, Xu S, Perry K, Frommer WB, Feng L. Structures of bacterial homologues of SWEET transporters in two distinct conformations. Nature. 2014 Sep 3. doi: 10.1038/nature13670. PMID:25186729 doi:http://dx.doi.org/10.1038/nature13670
- ↑ Latorraca NR, Fastman NM, Venkatakrishnan AJ, Frommer WB, Dror RO, Feng L. Mechanism of Substrate Translocation in an Alternating Access Transporter. Cell. 2017 Mar 23;169(1):96-107.e12. doi: 10.1016/j.cell.2017.03.010. PMID:28340354 doi:http://dx.doi.org/10.1016/j.cell.2017.03.010
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