2bt9: Difference between revisions
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== | ==Lectin from Ralstonia solanacearum complexed with Me-fucoside== | ||
Plant pathogens, like animal ones, use protein-carbohydrate interactions | <StructureSection load='2bt9' size='340' side='right'caption='[[2bt9]], [[Resolution|resolution]] 0.94Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2bt9]] 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=2BT9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BT9 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.94Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MFU:ALPHA-L-METHYL-FUCOSE'>MFU</scene></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=2bt9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bt9 OCA], [https://pdbe.org/2bt9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bt9 RCSB], [https://www.ebi.ac.uk/pdbsum/2bt9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bt9 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8XXK6_RALSO Q8XXK6_RALSO] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2bt9" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Ralstonia solanacearum]] | [[Category: Ralstonia solanacearum]] | ||
[[Category: Imberty A]] | |||
[[Category: Imberty | [[Category: Kostlanova N]] | ||
[[Category: Kostlanova | [[Category: Mitchell EP]] | ||
[[Category: Mitchell | [[Category: Wimmerova M]] | ||
[[Category: Wimmerova | |||
Latest revision as of 12:19, 9 May 2024
Lectin from Ralstonia solanacearum complexed with Me-fucosideLectin from Ralstonia solanacearum complexed with Me-fucoside
Structural highlights
FunctionPublication Abstract from PubMedPlant 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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