View source for 5bvu


==Crystal structure of Thermoanaerobacterium xylolyticum GH116 beta-glucosidase==
<StructureSection load='5bvu' size='340' side='right'caption='[[5bvu]], [[Resolution|resolution]] 1.61&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5bvu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoanaerobacterium_xylanolyticum_LX-11 Thermoanaerobacterium xylanolyticum LX-11]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BVU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BVU FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=5bvu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bvu OCA], [https://pdbe.org/5bvu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bvu RCSB], [https://www.ebi.ac.uk/pdbsum/5bvu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bvu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/F6BL85_THEXL F6BL85_THEXL] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Human glucosylcerebrosidase 2 (GBA2) of the CAZy family GH116 is responsible for the breakdown of glycosphingolipids on the cytoplasmic face of the endoplasmic reticulum and Golgi apparatus. Genetic defects in GBA2 result in spastic paraplegia and cerebellar ataxia, while cross-talk between GBA2 and GBA1 glucosylceramidases may affect Gaucher disease. Here, we report the first three-dimensional structure for any GH116 enzyme, Thermoanaerobacterium xylanolyticum TxGH116 beta-glucosidase, alone and in complex with diverse ligands. These structures allow identification of the glucoside binding and active site residues, which are shown to be conserved with GBA2. Mutagenic analysis of TxGH116 and structural modeling of GBA2 provide a detailed structural and functional rationale for pathogenic missense mutations of GBA2.

Bacterial beta-Glucosidase Reveals the Structural and Functional Basis of Genetic Defects in Human Glucocerebrosidase 2 (GBA2).,Charoenwattanasatien R, Pengthaisong S, Breen I, Mutoh R, Sansenya S, Hua Y, Tankrathok A, Wu L, Songsiriritthigul C, Tanaka H, Williams SJ, Davies GJ, Kurisu G, Cairns JR ACS Chem Biol. 2016 May 6. PMID:27115290<ref>PMID:27115290</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5bvu" style="background-color:#fffaf0;"></div>

==See Also==
*[[Beta-glucosidase 3D structures|Beta-glucosidase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermoanaerobacterium xylanolyticum LX-11]]
[[Category: Charoenwattanasatien R]]
[[Category: Ketudat Cairns JR]]
[[Category: Kurisu G]]
[[Category: Mutoh R]]
[[Category: Pengthaisong S]]
[[Category: Sansenya S]]
[[Category: Tanaka H]]