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2bs5

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==LECTIN FROM RALSTONIA SOLANACEARUM COMPLEXED WITH 2-FUCOSYLLACTOSE==
==LECTIN FROM RALSTONIA SOLANACEARUM COMPLEXED WITH 2-FUCOSYLLACTOSE==
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<StructureSection load='2bs5' size='340' side='right' caption='[[2bs5]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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<StructureSection load='2bs5' size='340' side='right'caption='[[2bs5]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2bs5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ralstonia_solanacearum Ralstonia solanacearum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BS5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BS5 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2bs5]] is a 1 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=2BS5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BS5 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<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=2bs5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bs5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bs5 RCSB], [http://www.ebi.ac.uk/pdbsum/2bs5 PDBsum]</span></td></tr>
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<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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=PRD_900070:2-fucosyllactose'>PRD_900070</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bs5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bs5 OCA], [https://pdbe.org/2bs5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bs5 RCSB], [https://www.ebi.ac.uk/pdbsum/2bs5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bs5 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A0A0S4TLR1_RALSL A0A0S4TLR1_RALSL]
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Plant pathogens, like animal ones, use protein-carbohydrate interactions in their strategy for host recognition, attachment, and invasion. The bacterium Ralstonia solanacearum, which is distributed worldwide and causes lethal wilt in many agricultural crops, was shown to produce a potent L-fucose-binding lectin, R. solanacearum lectin, a small protein of 90 amino acids with a tandem repeat in its amino acid sequence. In the present study, surface plasmon resonance experiments conducted on a series of oligosaccharides show a preference for binding to alphaFuc1-2Gal and alphaFuc1-6Gal epitopes. Titration microcalorimetry demonstrates the presence of two binding sites per monomer and an unusually high affinity of the lectin for alphaFuc1-2Gal-containing oligosaccharides (KD = 2.5 x 10(-7) M for 2-fucosyllactose). R. solanacearum lectin has been crystallized with a methyl derivative of fucose and with the highest affinity ligand, 2-fucosyllactose. X-ray crystal structures, the one with alpha-methyl-fucoside being at ultrahigh resolution, reveal that each monomer consists of two small four-stranded anti-parallel beta-sheets. Trimerization through a 3-fold or pseudo-3-fold axis generates a six-bladed beta-propeller architecture, very similar to that previously described for the fungal lectin of Aleuria aurantia. This is the first report of a beta-propeller formed by oligomerization and not by sequential domains. Each monomer presents two fucose binding sites, resulting in six symmetrically arranged sugar binding sites for the beta-propeller. Crystals were also obtained for a mutated lectin complexed with a fragment of xyloglucan, a fucosylated polysaccharide from the primary cell wall of plants, which may be the biological target of the lectin.
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The fucose-binding lectin from Ralstonia solanacearum. A new type of beta-propeller architecture formed by oligomerization and interacting with fucoside, fucosyllactose, and plant xyloglucan.,Kostlanova N, Mitchell EP, Lortat-Jacob H, Oscarson S, Lahmann M, Gilboa-Garber N, Chambat G, Wimmerova M, Imberty A J Biol Chem. 2005 Jul 29;280(30):27839-49. Epub 2005 May 27. PMID:15923179<ref>PMID:15923179</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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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Large Structures]]
[[Category: Ralstonia solanacearum]]
[[Category: Ralstonia solanacearum]]
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[[Category: Imberty, A]]
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[[Category: Imberty A]]
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[[Category: Kostlanova, N]]
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[[Category: Kostlanova N]]
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[[Category: Mitchell, E P]]
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[[Category: Mitchell EP]]
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[[Category: Wimmerova, M]]
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[[Category: Wimmerova M]]
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[[Category: Beta-propeller]]
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[[Category: Sugar binding protein]]
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[[Category: Sugar recognition]]
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Current revision

LECTIN FROM RALSTONIA SOLANACEARUM COMPLEXED WITH 2-FUCOSYLLACTOSE

PDB ID 2bs5

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