View source for 9sd5


==Crystal structure of the C-terminally truncated human E574Q-PGGHG mutant in complex with glucose==
<StructureSection load='9sd5' size='340' side='right'caption='[[9sd5]], [[Resolution|resolution]] 1.36&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9sd5]] is a 1 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=9SD5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9SD5 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]] 1.363&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=9sd5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9sd5 OCA], [https://pdbe.org/9sd5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9sd5 RCSB], [https://www.ebi.ac.uk/pdbsum/9sd5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9sd5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PGGHG_HUMAN PGGHG_HUMAN] Catalyzes the hydrolysis of glucose from the disaccharide unit linked to hydroxylysine residues of collagen and collagen-like proteins.<ref>PMID:26682924</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The enzyme glucosylgalactosylhydroxylysine glucosidase (PGGHG) plays a critical role in collagen metabolism by hydrolyzing the 2-O-alpha-d-glucopyranosyl-O-beta-d-galactopyranose, a natural disaccharide found in the glycosylation of hydroxylysine residues in collagen. We report the X-ray crystallographic structure of human PGGHG, revealing the canonical four-domain fold of enzymes from the GH65 family and representing the first structure reported for a mammalian enzyme in this family. A distinctive flat surface adjacent to the catalytic site, shaped by the N-terminal beta-sheet and specific conformations of catalytic loops, is unique to PGGHG among GH65 enzymes. Structural complexes with glucose and the substrate analogue kojibiose (KJB), along with site-directed mutagenesis and enzyme assays, identify residues critical for catalysis and hydroxylysine-collagen binding. Docking studies and AlphaFold3-based predictions suggest that the flat surface facilitates the contact between PGGHG and collagen peptides as well as substrate recognition, and support the enzyme's high specificity toward its glucosaccharide substrate. These findings provide structural insight into the selective recognition of glycosylated hydroxylysines and may inform future therapeutic or biotechnological applications targeting collagen metabolism.

The structure of human glucosidase PGGHG reveals a very specific active site accessible through a flat surface for collagen approximation.,Casas-Florez D, Ortega-Garcia R, Sanz-Benito P, Monterroso B, Sanz-Aparicio J, Gonzalez B Int J Biol Macromol. 2026 Feb;345:150556. doi: 10.1016/j.ijbiomac.2026.150556. , Epub 2026 Jan 26. PMID:41605404<ref>PMID:41605404</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9sd5" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Casas-Florez D]]
[[Category: Gonzalez B]]
[[Category: Ortega-Garcia R]]
[[Category: Sanz-Aparicio J]]