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| | ==Structure of RSL mutant W76A in complex with L-fucose== | | ==Structure of RSL mutant W76A in complex with L-fucose== |
| - | <StructureSection load='4i6s' size='340' side='right' caption='[[4i6s]], [[Resolution|resolution]] 1.54Å' scene=''> | + | <StructureSection load='4i6s' size='340' side='right'caption='[[4i6s]], [[Resolution|resolution]] 1.54Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4i6s]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_solanacearum"_smith_1896 "bacillus solanacearum" smith 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I6S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4I6S FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4i6s]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Ralstonia_solanacearum Ralstonia solanacearum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I6S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4I6S FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2bt9|2bt9]]</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=4i6s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i6s OCA], [https://pdbe.org/4i6s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4i6s RCSB], [https://www.ebi.ac.uk/pdbsum/4i6s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4i6s ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CMR15_11270, rsc2107 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=305 "Bacillus solanacearum" Smith 1896])</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=4i6s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i6s OCA], [http://pdbe.org/4i6s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4i6s RCSB], [http://www.ebi.ac.uk/pdbsum/4i6s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4i6s ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/D8NA05_RALSL D8NA05_RALSL] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus solanacearum smith 1896]] | + | [[Category: Large Structures]] |
| - | [[Category: Arnaud, J]] | + | [[Category: Ralstonia solanacearum]] |
| - | [[Category: Audfray, A]] | + | [[Category: Arnaud J]] |
| - | [[Category: Imberty, A]] | + | [[Category: Audfray A]] |
| - | [[Category: Varrot, A]] | + | [[Category: Imberty A]] |
| - | [[Category: Beta-propeller]]
| + | [[Category: Varrot A]] |
| - | [[Category: Fucosylated oligosaccharides binding]]
| + | |
| - | [[Category: L-fucose]]
| + | |
| - | [[Category: Lectin]]
| + | |
| - | [[Category: Multivalency]]
| + | |
| - | [[Category: Soluble]]
| + | |
| - | [[Category: Sugar binding protein]]
| + | |
| - | [[Category: Trivalent fucose binding lectin]]
| + | |
| Structural highlights
Function
D8NA05_RALSL
Publication Abstract from PubMed
Multivalency is proposed to play a role in the strong avidity of lectins for glycosylated cell surfaces and also in their ability to affect membrane dynamics by clustering glycosphingolipids. Lectins with modified valency were designed from the beta-propeller fold of Ralstonia solanacearum lectin (RSL) that presents six fucose binding sites. After identification of key amino acids by molecular dynamics calculations, two mutants with reduced valency were produced. Isothermal titration calorimetry confirmed the loss of three high affinity binding sites for both mutants. Crystal structures indicated that residual low affinity binding occurred in W76A but not in R17A. The trivalent R17A mutant presented unchanged avidity toward fucosylated surfaces, when compared to hexavalent RSL. However, R17A is not able anymore to induce formation of membrane invaginations on giant unilamellar vesicules, indicating the crucial role of number of binding sites for clustering of glycolipids. In the human lung epithelial cell line H1299, wt-RSL is internalized within seconds whereas the kinetics of R17A uptake is largely delayed. Neolectins with tailored valency are promising tools to study membrane dynamics.
Reduction of Lectin Valency Drastically Changes Glycolipid Dynamics in Membranes but Not Surface Avidity.,Arnaud J, Claudinon J, Trondle K, Trovaslet M, Larson G, Thomas A, Varrot A, Romer W, Imberty A, Audfray A ACS Chem Biol. 2013 Jul 23. PMID:23855446[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Arnaud J, Claudinon J, Trondle K, Trovaslet M, Larson G, Thomas A, Varrot A, Romer W, Imberty A, Audfray A. Reduction of Lectin Valency Drastically Changes Glycolipid Dynamics in Membranes but Not Surface Avidity. ACS Chem Biol. 2013 Jul 23. PMID:23855446 doi:10.1021/cb400254b
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