6tq5: Difference between revisions
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==Alcohol dehydrogenase from Candida magnoliae DSMZ 70638 (ADHA): complex with NADP+== | |||
<StructureSection load='6tq5' size='340' side='right'caption='[[6tq5]], [[Resolution|resolution]] 1.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6tq5]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TQ5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6TQ5 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></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=6tq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tq5 OCA], [http://pdbe.org/6tq5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6tq5 RCSB], [http://www.ebi.ac.uk/pdbsum/6tq5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6tq5 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> | ||
<div class="pdbe-citations 6tq5" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Aalbers, F S]] | |||
[[Category: Fraaije, M W]] | |||
[[Category: Mattevi, A]] | |||
[[Category: Rovida, S]] | [[Category: Rovida, S]] | ||
[[Category: | [[Category: Alcohol dehydrogenase]] | ||
[[Category: | [[Category: Oxidoreductase]] | ||
[[Category: | [[Category: Protein engineering]] | ||
[[Category: Thermal stability]] | |||
