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==Crystal structure of alpha-L-fucosidase from Vibrio sp. strain EJY3==
<StructureSection load='7db5' size='340' side='right'caption='[[7db5]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DB5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DB5 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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=7db5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7db5 OCA], [https://pdbe.org/7db5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7db5 RCSB], [https://www.ebi.ac.uk/pdbsum/7db5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7db5 ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Carbohydrates are structurally and functionally diverse materials including polysaccharides, and marine organisms are known to have many enzymes for the breakdown of complex polysaccharides. Here, we identified an alpha-l-fucosidase enzyme from the marine bacterium Vibrio sp. strain EJY3 (VejFCD) that has dual alpha-1,4-glucosidic and beta-1,4-galactosidic specificities. We determined the crystal structure of VejFCD and provided the structural basis underlying the dual alpha- and beta-glycosidase activities of the enzyme. Unlike other three-domain FCDs, in VejFCD, carbohydrate-binding module-B (CBM-B) with a novel beta-sandwich fold tightly contacts with the CatD/CBM-B main body and provides key residues for the beta-1,4-glycosidase activity of the enzyme. The phylogenetic tree analysis suggests that only a few FCDs from marine microorganisms have the key structural features for dual alpha-1,4- and beta-1,4-glycosidase activities. This study provides the structural insights into the mechanism underlying the novel glycoside hydrolase activities and could be applied for more efficient utilization in the hydrolysis of complex carbohydrates in biotechnological applications.

Dual alpha-1,4- and beta-1,4-Glycosidase Activities by the Novel Carbohydrate-Binding Module in alpha-l-Fucosidase from Vibrio sp. Strain EJY3.,Hong H, Kim DH, Seo H, Kim KH, Kim KJ J Agric Food Chem. 2021 Mar 11. doi: 10.1021/acs.jafc.0c08199. PMID:33705122<ref>PMID:33705122</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Hong H]]
[[Category: Kim K-J]]