View source for 9pnj


==Crystal structure of the GH29-like fucosidase FucWf4==
<StructureSection load='9pnj' size='340' side='right'caption='[[9pnj]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9pnj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Wenyingzhuangia_fucanilytica Wenyingzhuangia fucanilytica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9PNJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9PNJ 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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=9pnj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9pnj OCA], [https://pdbe.org/9pnj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9pnj RCSB], [https://www.ebi.ac.uk/pdbsum/9pnj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9pnj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A1B1Y5Q3_9FLAO A0A1B1Y5Q3_9FLAO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Fucoidan is a complex, sulfated polysaccharide primarily found in brown algae, where it plays important structural and protective roles. Due to its abundance in marine ecosystems, many marine bacteria have evolved diverse and specialized enzymatic systems to degrade fucoidan, although the functions and structures of many of these enzymes remain uncharacterized. Here, we describe the structure of a newly identified fucosidase, FucWf4, which cleaves terminal, unsulfated fucose residues from linear, sulfated fucoidan. FucWf4 does not belong to any known glycoside hydrolase (GH) family, but shows the greatest similarity to GH29 fucosidases. We present the first crystal structure of FucWf4 in complex with fucose, revealing a unique C-terminal domain that resembles a carbohydrate-binding module, although it may have lost its carbohydrate-binding capacity and is absent from canonical GH29 enzymes. Docking experiments suggest the presence of a -1 subsite containing a potential sulfate-binding pocket, which may underlie the substrate specificity of the enzyme. Furthermore, sequence analysis of FucWf4 homologs reveals two distinct clades, likely corresponding to functionally divergent groups. Together, these findings provide new insights into the molecular basis of fucoidan recognition and degradation by this novel enzyme subfamily, laying the groundwork for future functional and structural studies.

Structural insights into a fucosidase involved in fucoidan degradation.,Bailey B, Winchester A, McClain D, Clingaman M, Higgins MA Acta Crystallogr F Struct Biol Commun. 2025 Nov 1;81(Pt 11):459-466. doi: , 10.1107/S2053230X25008842. Epub 2025 Oct 20. PMID:41114657<ref>PMID:41114657</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9pnj" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Wenyingzhuangia fucanilytica]]
[[Category: Higgins MA]]