View source for 7pls


==Cryo-EM structures of human fucosidase FucA1 reveal insight into substate recognition and catalysis.==
<StructureSection load='7pls' size='340' side='right'caption='[[7pls]], [[Resolution|resolution]] 2.49&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7pls]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PLS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PLS FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.49&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=7pls FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pls OCA], [https://pdbe.org/7pls PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pls RCSB], [https://www.ebi.ac.uk/pdbsum/7pls PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pls ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/FUCO_HUMAN FUCO_HUMAN] Fucosidosis. The disease is caused by variants affecting the gene represented in this entry.
== Function ==
[https://www.uniprot.org/uniprot/FUCO_HUMAN FUCO_HUMAN] Alpha-L-fucosidase is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins.<ref>PMID:9741689</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Enzymatic hydrolysis of alpha-L-fucose from fucosylated glycoconjugates is consequential in bacterial infections and the neurodegenerative lysosomal storage disorder fucosidosis. Understanding human alpha-L-fucosidase catalysis, in an effort toward drug design, has been hindered by the absence of three-dimensional structural data for any animal fucosidase. Here, we have used cryoelectron microscopy (cryo-EM) to determine the structure of human lysosomal alpha-L-fucosidase (FucA1) in both an unliganded state and in complex with the inhibitor deoxyfuconojirimycin. These structures, determined at 2.49 A resolution, reveal the homotetrameric structure of FucA1, the architecture of the catalytic center, and the location of both natural population variations and disease-causing mutations. Furthermore, this work has conclusively identified the hitherto contentious identity of the catalytic acid/base as aspartate-276, representing a shift from both the canonical glutamate acid/base residue and a previously proposed glutamate residue. These findings have furthered our understanding of how FucA1 functions in both health and disease.

Cryo-EM structures of human fucosidase FucA1 reveal insight into substrate recognition and catalysis.,Armstrong Z, Meek RW, Wu L, Blaza JN, Davies GJ Structure. 2022 Oct 6;30(10):1443-1451.e5. doi: 10.1016/j.str.2022.07.001. Epub , 2022 Jul 29. PMID:35907402<ref>PMID:35907402</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7pls" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Armstrong Z]]
[[Category: Blaza JN]]
[[Category: Davies GJ]]
[[Category: Meek RW]]
[[Category: Wu L]]