6tq3: Difference between revisions
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==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 with sequence from [https://en.wikipedia.org/wiki/Starmerella_magnoliae Starmerella magnoliae]. 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 [https://proteopedia.org/fgij/fg.htm?mol=6TQ3 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]] 2Å</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=6tq3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tq3 OCA], [https://pdbe.org/6tq3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tq3 RCSB], [https://www.ebi.ac.uk/pdbsum/6tq3 PDBsum], [https://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 | == References == | ||
[[Category: Mattevi | <references/> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Starmerella magnoliae]] | |||
[[Category: Aalbers FS]] | |||
[[Category: Fraaije MW]] | |||
[[Category: Mattevi A]] | |||
[[Category: Rovida S]] | |||
Latest revision as of 13:07, 24 January 2024
Alcohol dehydrogenase from Candida magnoliae DSMZ 70638 (ADHA)
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