View source for 5d06


==Crystal Structure of the Candida Glabrata Glycogen Debranching Enzyme==
<StructureSection load='5d06' size='340' side='right'caption='[[5d06]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5d06]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_glabrata_CBS_138 Candida glabrata CBS 138]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D06 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D06 FirstGlance]. <br>
</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=5d06 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d06 OCA], [https://pdbe.org/5d06 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d06 RCSB], [https://www.ebi.ac.uk/pdbsum/5d06 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d06 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q6FSK0_CANGA Q6FSK0_CANGA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Glycogen is a branched glucose polymer and serves as an important energy store. Its debranching is a critical step in its mobilization. In animals and fungi, the 170 kDa glycogen debranching enzyme (GDE) catalyses this reaction. GDE deficiencies in humans are associated with severe diseases collectively termed glycogen storage disease type III (GSDIII). We report crystal structures of GDE and its complex with oligosaccharides, and structure-guided mutagenesis and biochemical studies to assess the structural observations. These studies reveal that distinct domains in GDE catalyse sequential reactions in glycogen debranching, the mechanism of their catalysis and highly specific substrate recognition. The unique tertiary structure of GDE provides additional contacts to glycogen besides its active sites, and our biochemical experiments indicate that they mediate its recruitment to glycogen and regulate its activity. Combining the understanding of the GDE catalysis and functional characterizations of its disease-causing mutations provides molecular insights into GSDIII.

Crystal structure of glycogen debranching enzyme and insights into its catalysis and disease-causing mutations.,Zhai L, Feng L, Xia L, Yin H, Xiang S Nat Commun. 2016 Apr 18;7:11229. doi: 10.1038/ncomms11229. PMID:27088557<ref>PMID:27088557</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5d06" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Xiang S]]
[[Category: Zhai L]]