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| | ==Structure of BambL lectin from Burkholderia ambifaria== | | ==Structure of BambL lectin from Burkholderia ambifaria== |
| - | <StructureSection load='3zw0' size='340' side='right' caption='[[3zw0]], [[Resolution|resolution]] 1.60Å' scene=''> | + | <StructureSection load='3zw0' size='340' side='right'caption='[[3zw0]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3zw0]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Burkholderia_ambifaria Burkholderia ambifaria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZW0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZW0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3zw0]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_ambifaria_AMMD Burkholderia ambifaria AMMD]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZW0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZW0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</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]] 1.6Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MHO:S-OXYMETHIONINE'>MHO</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MHO:S-OXYMETHIONINE'>MHO</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3zw2|3zw2]], [[3zw1|3zw1]], [[3zwe|3zwe]], [[3zzv|3zzv]]</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=3zw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zw0 OCA], [https://pdbe.org/3zw0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zw0 RCSB], [https://www.ebi.ac.uk/pdbsum/3zw0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zw0 ProSAT]</span></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=3zw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zw0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zw0 RCSB], [http://www.ebi.ac.uk/pdbsum/3zw0 PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q0B4G1_BURCM Q0B4G1_BURCM] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 3zw0" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Burkholderia ambifaria]] | + | [[Category: Burkholderia ambifaria AMMD]] |
| - | [[Category: Abounit, S]] | + | [[Category: Large Structures]] |
| - | [[Category: Audfray, A]] | + | [[Category: Abounit S]] |
| - | [[Category: Claudinon, J]] | + | [[Category: Audfray A]] |
| - | [[Category: Imberty, A]] | + | [[Category: Claudinon J]] |
| - | [[Category: Larson, G]] | + | [[Category: Imberty A]] |
| - | [[Category: Lependu, J]] | + | [[Category: Larson G]] |
| - | [[Category: Romer, W]] | + | [[Category: LePendu J]] |
| - | [[Category: Ruvoen-Clouet, N]] | + | [[Category: Romer W]] |
| - | [[Category: Varrot, A]] | + | [[Category: Ruvoen-Clouet N]] |
| - | [[Category: Wimmerova, M]] | + | [[Category: Varrot A]] |
| - | [[Category: B-propeller]]
| + | [[Category: Wimmerova M]] |
| - | [[Category: Cystic fibrosis]]
| + | |
| - | [[Category: Human histo-blood group]]
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| - | [[Category: Sugar binding protein]]
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| Structural highlights
Function
Q0B4G1_BURCM
Publication Abstract from PubMed
Burkholderia ambifaria is generally associated with the rhizosphere of plants where it has biocontrol effects on other microorganisms. It is also a member of the Burkholderia cepacia complex, a group of closely related bacteria that cause lung infections in immunocompromised patients as well as in patients with granulomatous disease or cystic fibrosis. Our previous work indicated that fucose on human epithelia is a frequent target for lectins and adhesins of lung pathogens (Sulak, O., Cioci, G., Lameignere, E., Balloy, V., Round, A., Gutsche, I., Malinovska, L., Chignard, M., Kosma, P., Aubert, D. F., Marolda, C. L., Valvano, M. A., Wimmerova, M., and Imberty, A. (2011) PLoS Pathog. 7, e1002238). Analysis of the B. ambifaria genome identified BambL as a putative fucose-binding lectin. The 87-amino acid protein was produced recombinantly and demonstrated to bind to fucosylated oligosaccharides with a preference for alphaFuc1-2Gal epitopes. Crystal structures revealed that it associates as a trimer with two fucose-binding sites per monomer. The overall fold is a six-bladed beta-propeller formed by oligomerization as in the Ralstonia solanacearum lectin and not by sequential domains like the fungal fucose lectin from Aleuria aurantia. The affinity of BambL for small fucosylated glycans is very high as demonstrated by microcalorimetry (K(D) < 1 mum). Plant cell wall oligosaccharides and human histo-blood group oligosaccharides H-type 2 and Lewis Y are bound with equivalent efficiency. Binding to artificial glycosphingolipid-containing vesicles, human saliva, and lung tissues confirmed that BambL could recognize a wide spectrum of fucosylated epitopes, albeit with a lower affinity for biological material from nonsecretor individuals.
Fucose-binding Lectin from Opportunistic Pathogen Burkholderia ambifaria Binds to Both Plant and Human Oligosaccharidic Epitopes.,Audfray A, Claudinon J, Abounit S, Ruvoen-Clouet N, Larson G, Smith DF, Wimmerova M, Le Pendu J, Romer W, Varrot A, Imberty A J Biol Chem. 2012 Feb 3;287(6):4335-47. Epub 2011 Dec 14. PMID:22170069[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Audfray A, Claudinon J, Abounit S, Ruvoen-Clouet N, Larson G, Smith DF, Wimmerova M, Le Pendu J, Romer W, Varrot A, Imberty A. Fucose-binding Lectin from Opportunistic Pathogen Burkholderia ambifaria Binds to Both Plant and Human Oligosaccharidic Epitopes. J Biol Chem. 2012 Feb 3;287(6):4335-47. Epub 2011 Dec 14. PMID:22170069 doi:10.1074/jbc.M111.314831
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