4aio
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Crystal structure of the starch debranching enzyme barley limit dextrinase== | |
+ | <StructureSection load='4aio' size='340' side='right'caption='[[4aio]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[4aio]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AIO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AIO 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]] 1.9Å</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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</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=4aio FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aio OCA], [https://pdbe.org/4aio PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4aio RCSB], [https://www.ebi.ac.uk/pdbsum/4aio PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4aio ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/O48541_HORVV O48541_HORVV] | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Barley limit dextrinase (HvLD) is a debranching enzyme from glycoside hydrolase family 13 subfamily 13 (GH13_13) that hydrolyses alpha-1,6-glucosidic linkages in limit dextrins derived from amylopectin. The structure of HvLD was solved and refined to 1.9 A resolution. The structure has a glycerol molecule in the active site and is virtually identical to the structures of HvLD in complex with the competitive inhibitors alpha-cyclodextrin and beta-cyclodextrin solved to 2.5 and 2.1 A resolution, respectively. However, three loops in the N-terminal domain that are shown here to resemble carbohydrate-binding module family 21 were traceable and were included in the present HvLD structure but were too flexible to be traced and included in the structures of the two HvLD-inhibitor complexes. | ||
- | + | Structure of the starch-debranching enzyme barley limit dextrinase reveals homology of the N-terminal domain to CBM21.,Moller MS, Abou Hachem M, Svensson B, Henriksen A Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Sep;68(Pt 9):1008-12. Epub, 2012 Aug 29. PMID:22949184<ref>PMID:22949184</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
+ | </div> | ||
+ | <div class="pdbe-citations 4aio" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Hordeum vulgare]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Abou Hachem M]] | ||
+ | [[Category: Henriksen A]] | ||
+ | [[Category: Moeller MS]] | ||
+ | [[Category: Svensson B]] |
Current revision
Crystal structure of the starch debranching enzyme barley limit dextrinase
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