This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
6tq8
From Proteopedia
(Difference between revisions)
m (Protected "6tq8" [edit=sysop:move=sysop]) |
|||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Alcohol dehydrogenase from Candida magnoliae DSMZ 70638 (ADHA): thermostable 10fold mutant== | |
| + | <StructureSection load='6tq8' size='340' side='right'caption='[[6tq8]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6tq8]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TQ8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6TQ8 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=6tq8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tq8 OCA], [http://pdbe.org/6tq8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6tq8 RCSB], [http://www.ebi.ac.uk/pdbsum/6tq8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6tq8 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 6tq8" 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 06:56, 8 April 2020
Alcohol dehydrogenase from Candida magnoliae DSMZ 70638 (ADHA): thermostable 10fold mutant
| |||||||||||
