8b97: Difference between revisions
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==N-terminal beta-trefoil lectin domain of the Laccaria bicolor lectin in complex with N-acetyl-lactosamine== | |||
<StructureSection load='8b97' size='340' side='right'caption='[[8b97]], [[Resolution|resolution]] 0.97Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8b97]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Laccaria_bicolor_S238N-H53 Laccaria bicolor S238N-H53]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8B97 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8B97 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PRD_900019:N-acetyl-alpha-lactosamine'>PRD_900019</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=8b97 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8b97 OCA], [https://pdbe.org/8b97 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8b97 RCSB], [https://www.ebi.ac.uk/pdbsum/8b97 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8b97 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/B0D650_LACBS B0D650_LACBS] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Lectins from fruiting bodies are a diverse group of sugar-binding proteins from mushrooms that face the biologically relevant challenge of discriminating self- from non-self carbohydrate structures, therefore providing a basis for an innate defence system. Such a system entails both detection and destruction of invaders and/or feeders, and in contrast to more complex organisms with immense immune systems, these two functions normally rely on multitasking lectins, namely, lectins with different functional modules. Here, we present a novel fungal lectin, LBL, from the basidiomycete Laccaria bicolor. Using a diverse set of biophysical techniques, we unveil the fine details of the sugar-binding specificity of the N-terminal beta-trefoil of LBL (LBL(152)), whose structure has been determined at the highest resolution so far reported for such a fold. LBL(152) binds complex poly-N-Acetyllactosamine polysaccharides and also robust LBL(152) binding to Caenorhabditis elegans and Drosophila melanogaster cellular extracts was detected in microarray assays, with a seeming preference for the fruit fly adult and pupa stages over the larva stage. Prediction of the structure of the C-terminal part of LBL with AlphaFold reveals a tandem repeat of two structurally almost identical domains of around 110 amino acids each, despite sharing low sequence conservation. | |||
Atomic crystal structure and sugar specificity of a beta-trefoil lectin domain from the ectomycorrhizal basidiomycete Laccaria bicolor.,Acebron I, Campanero-Rhodes MA, Solis D, Menendez M, Garcia C, Lillo MP, Mancheno JM Int J Biol Macromol. 2023 Feb 7;233:123507. doi: 10.1016/j.ijbiomac.2023.123507. PMID:36754262<ref>PMID:36754262</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 8b97" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Laccaria bicolor S238N-H53]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Acebron I]] | |||
[[Category: Campanero-Rhodes MA]] | |||
[[Category: Garcia C]] | |||
[[Category: Lillo MP]] | |||
[[Category: Mancheno JM]] | |||
[[Category: Menendez M]] | |||
[[Category: Solis D]] | |||
Revision as of 15:40, 22 February 2023
N-terminal beta-trefoil lectin domain of the Laccaria bicolor lectin in complex with N-acetyl-lactosamineN-terminal beta-trefoil lectin domain of the Laccaria bicolor lectin in complex with N-acetyl-lactosamine
Structural highlights
FunctionPublication Abstract from PubMedLectins from fruiting bodies are a diverse group of sugar-binding proteins from mushrooms that face the biologically relevant challenge of discriminating self- from non-self carbohydrate structures, therefore providing a basis for an innate defence system. Such a system entails both detection and destruction of invaders and/or feeders, and in contrast to more complex organisms with immense immune systems, these two functions normally rely on multitasking lectins, namely, lectins with different functional modules. Here, we present a novel fungal lectin, LBL, from the basidiomycete Laccaria bicolor. Using a diverse set of biophysical techniques, we unveil the fine details of the sugar-binding specificity of the N-terminal beta-trefoil of LBL (LBL(152)), whose structure has been determined at the highest resolution so far reported for such a fold. LBL(152) binds complex poly-N-Acetyllactosamine polysaccharides and also robust LBL(152) binding to Caenorhabditis elegans and Drosophila melanogaster cellular extracts was detected in microarray assays, with a seeming preference for the fruit fly adult and pupa stages over the larva stage. Prediction of the structure of the C-terminal part of LBL with AlphaFold reveals a tandem repeat of two structurally almost identical domains of around 110 amino acids each, despite sharing low sequence conservation. Atomic crystal structure and sugar specificity of a beta-trefoil lectin domain from the ectomycorrhizal basidiomycete Laccaria bicolor.,Acebron I, Campanero-Rhodes MA, Solis D, Menendez M, Garcia C, Lillo MP, Mancheno JM Int J Biol Macromol. 2023 Feb 7;233:123507. doi: 10.1016/j.ijbiomac.2023.123507. PMID:36754262[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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