7ekw
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of the Candida Glabrata Glycogen Debranching Enzyme (D535N) in complex with maltotetrose== | |
| + | <StructureSection load='7ekw' size='340' side='right'caption='[[7ekw]], [[Resolution|resolution]] 3.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7ekw]] 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=7EKW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EKW 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]] 3.1Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</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=7ekw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ekw OCA], [https://pdbe.org/7ekw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ekw RCSB], [https://www.ebi.ac.uk/pdbsum/7ekw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ekw ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q6FSK0_CANGA Q6FSK0_CANGA] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Debranching is a critical step in the mobilization of the important energy store glycogen. In eukaryotes, including fungi and animals, the highly conserved glycogen-debranching enzyme (GDE) debranches glycogen by a glucanotransferase (GT) reaction followed by a glucosidase (GC) reaction. Previous work indicated that these reactions are catalyzed by two active sites located more than 50 A apart and provided insights into their catalytic mechanisms and substrate recognition. Here, five crystal structures of GDE in complex with oligosaccharides with 4-9 glucose residues are presented. The data suggest that the glycogen main chain plays a critical role in binding to the GT and GC active sites of GDE and that a minimum of five main-chain residues are required for optimal binding. | ||
| - | + | Crystal structures of glycogen-debranching enzyme mutants in complex with oligosaccharides.,Shen M, Gong X, Xiang S Acta Crystallogr F Struct Biol Commun. 2021 Nov 1;77(Pt 11):420-426. doi:, 10.1107/S2053230X21010918. Epub 2021 Oct 29. PMID:34726181<ref>PMID:34726181</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 7ekw" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Shen M]] | ||
| + | [[Category: Xiang S]] | ||
Current revision
Crystal Structure of the Candida Glabrata Glycogen Debranching Enzyme (D535N) in complex with maltotetrose
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