5oc3
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Ser67Cys/Pro121Cys Amadoriase I mutant from Aspergillus Fumigatus== | |
| + | <StructureSection load='5oc3' size='340' side='right' caption='[[5oc3]], [[Resolution|resolution]] 2.15Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5oc3]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OC3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OC3 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5oc3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oc3 OCA], [http://pdbe.org/5oc3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5oc3 RCSB], [http://www.ebi.ac.uk/pdbsum/5oc3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5oc3 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Amadoriases are a class of FAD-dependent enzymes that are found in fungi, yeast and bacteria and that are able to hydrolyze glycated amino acids, cleaving the sugar moiety from the amino acidic portion. So far, engineered Amadoriases have mostly found practical application in the measurement of the concentration of glycated albumin in blood samples. However, these engineered forms of Amadoriases show relatively low absolute activity and stability levels, which affect their conditions of use. Therefore, enzyme stabilization is desirable prior to function-altering molecular engineering. In this work, we describe a rational design strategy based on a computational screening method to evaluate a library of potentially stabilizing disulfide bonds. Our approach allowed the identification of two thermostable Amadoriase I mutants (SS03 and SS17) featuring a significantly higher T50 (55.3 degrees C and 60.6 degrees C, respectively) compared to the wild-type enzyme (52.4 degrees C). Moreover, SS17 shows clear hyperstabilization, with residual activity up to 95 degrees C, whereas the wild-type enzyme is fully inactive at 55 degrees C. Our computational screening method can therefore be considered as a promising approach to expedite the design of thermostable enzymes. | ||
| - | + | Thermal stabilization of the deglycating enzyme Amadoriase I by rational design.,Rigoldi F, Donini S, Giacomina F, Sorana F, Redaelli A, Bandiera T, Parisini E, Gautieri A Sci Rep. 2018 Feb 14;8(1):3042. doi: 10.1038/s41598-018-19991-x. PMID:29445091<ref>PMID:29445091</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5oc3" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Donini, S]] | ||
| + | [[Category: Gautieri, A]] | ||
| + | [[Category: Parisini, E]] | ||
| + | [[Category: Rigoldi, F]] | ||
| + | [[Category: Flavin dependant enzyme]] | ||
| + | [[Category: Glycated aminoacid]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Thermoresistance]] | ||
Revision as of 06:20, 28 February 2018
Crystal structure of Ser67Cys/Pro121Cys Amadoriase I mutant from Aspergillus Fumigatus
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