6tq3
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Alcohol dehydrogenase from Candida magnoliae DSMZ 70638 (ADHA)== | |
| + | <StructureSection load='6tq3' size='340' side='right'caption='[[6tq3]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6tq3]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TQ3 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6TQ3 FirstGlance]. <br> | ||
| + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6tq3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tq3 OCA], [http://pdbe.org/6tq3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6tq3 RCSB], [http://www.ebi.ac.uk/pdbsum/6tq3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6tq3 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Enzyme instability is an important limitation for the investigation and application of enzymes. Therefore, methods to rapidly and effectively improve enzyme stability are highly appealing. In this study we applied a computational method (FRESCO) to guide the engineering of an alcohol dehydrogenase. Of the 177 selected mutations, 25 mutations brought about a significant increase in apparent melting temperature (DeltaTm >/= +3 degrees C). By combining mutations, a 10-fold mutant was generated with a Tm of 94 degrees C (+51 degrees C relative to wildtype), almost reaching water's boiling point, and the highest increase with FRESCO to date. The 10-fold mutant's structure was elucidated, which enabled the identification of an activity-impairing mutation. After reverting this mutation, the enzyme showed no loss in activity compared to wildtype, while displaying a Tm of 88 degrees C (+45 degrees C relative to wildtype). This work demonstrates the value of enzyme stabilization through computational library design. | ||
| - | + | Approaching boiling point stability of an alcohol dehydrogenase through computationally-guided enzyme engineering.,Aalbers FS, Furst MJ, Rovida S, Trajkovic M, Gomez Castellanos JR, Bartsch S, Vogel A, Mattevi A, Fraaije MW Elife. 2020 Mar 31;9. pii: 54639. doi: 10.7554/eLife.54639. PMID:32228861<ref>PMID:32228861</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 6tq3" style="background-color:#fffaf0;"></div> |
| - | [[Category: Fraaije, M | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Aalbers, F S]] | ||
| + | [[Category: Fraaije, M W]] | ||
[[Category: Mattevi, A]] | [[Category: Mattevi, A]] | ||
| - | [[Category: | + | [[Category: Rovida, S]] |
| + | [[Category: Alcohol dehydrogenase]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Protein engineering]] | ||
| + | [[Category: Thermal stability]] | ||
Revision as of 06:55, 8 April 2020
Alcohol dehydrogenase from Candida magnoliae DSMZ 70638 (ADHA)
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