4r27
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of beta-glycosidase BGL167== | |
| + | <StructureSection load='4r27' size='340' side='right'caption='[[4r27]], [[Resolution|resolution]] 2.03Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4r27]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Microbacterium_sp._Gsoil167 Microbacterium sp. Gsoil167]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R27 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R27 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]] 2.03Å</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=4r27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r27 OCA], [https://pdbe.org/4r27 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r27 RCSB], [https://www.ebi.ac.uk/pdbsum/4r27 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r27 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/L0ELG0_9MICO L0ELG0_9MICO] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Triterpenoids with desired glycosylation patterns have attracted considerable attention as potential therapeutics for inflammatory diseases and various types of cancer. Sugar-hydrolyzing enzymes with high substrate specificity would be far more efficient than other methods for the synthesis of such specialty triterpenoids, but they are yet to be developed. Here we present a strategy to rationally design a beta-glycosidase with high regiospecificity for triterpenoids. A beta-glycosidase with broad substrate specificity was isolated, and its crystal structure was determined at 2.0 A resolution. Based on the product profiles and substrate docking simulations, we modeled the substrate binding modes of the enzyme. From the model, the substrate binding cleft of the enzyme was redesigned in a manner that preferentially hydrolyzes glycans at specific glycosylation sites of triterpenoids. The designed mutants were shown to produce a variety of specialty triterpenoids with high purity. | ||
| - | + | Rational design of a beta-glycosidase with high regiospecificity for triterpenoid tailoring.,Park SJ, Choi JM, Kyeong HH, Kim SG, Kim HS Chembiochem. 2015 Mar 23;16(5):854-60. doi: 10.1002/cbic.201500004. Epub 2015 Feb, 20. PMID:25703680<ref>PMID:25703680</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 4r27" style="background-color:#fffaf0;"></div> |
| - | [[Category: Choi | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: Kyeong | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| + | [[Category: Large Structures]] | ||
| + | [[Category: Microbacterium sp. Gsoil167]] | ||
| + | [[Category: Choi JM]] | ||
| + | [[Category: Kim HS]] | ||
| + | [[Category: Kim SG]] | ||
| + | [[Category: Kyeong HH]] | ||
| + | [[Category: Park SJ]] | ||
Current revision
Crystal structure of beta-glycosidase BGL167
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