9s7k: Difference between revisions
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==INCYPRO crosslinked dimer of the D-stereospecific hydrolase dHy1== | |||
<StructureSection load='9s7k' size='340' side='right'caption='[[9s7k]], [[Resolution|resolution]] 1.77Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9s7k]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_thuringiensis Bacillus thuringiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9S7K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9S7K 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]] 1.771Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZIZ:~{N}-[2-[3,5-bis[2-(2-iodanylethanoylamino)ethanoyl]-1,3,5-triazinan-1-yl]-2-oxidanylidene-ethyl]-2-iodanyl-ethanamide'>ZIZ</scene></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=9s7k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9s7k OCA], [https://pdbe.org/9s7k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9s7k RCSB], [https://www.ebi.ac.uk/pdbsum/9s7k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9s7k ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Enzymes are powerful catalysts for selective transformations but often suffer from limited stability under operational conditions such as elevated temperature or the presence of organic cosolvents. While sequence-based strategies have been widely used to improve stability, chemical protein engineering enables modifications beyond the natural amino acid repertoire thereby offering complementary routes to tailor enzyme function and robustness. Here, we apply the in situ cyclization of proteins (INCYPRO) to a D-stereospecific hydrolase with low intrinsic thermal stability. Site-specific macrocyclization substantially improved resilience to heat and cosolvent stress. Unexpectedly, we discovered a cross-linked protein dimer with enhanced activity and thermal stability. The complex structure was confirmed by x-ray crystallography. Extending the INCYPRO approach, we engineered a multicyclic enzyme dimer with a total of four cross-linking sites, which not only retained high activity under benign conditions but also outperformed the wild-type under stress. Our findings establish protein macrocyclization as a versatile strategy to stabilize both monomeric and multimeric enzymes, providing a powerful route to robust biocatalysts. | |||
Multicyclic D-Stereospecific Hydrolase Dimer With High Sustained Activity.,Haim A, Liebscher S, Klintrot R, Vallino L, Masman M, Simon AH, Hahn M, Hennig S, Neubacher S, Bordusa F, Grossmann TN Angew Chem Int Ed Engl. 2026 Mar 20:e21611. doi: 10.1002/anie.202521611. PMID:41858178<ref>PMID:41858178</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 9s7k" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus thuringiensis]] | |||
[[Category: Large Structures]] | |||
[[Category: Bordusa F]] | |||
[[Category: Grossmann TN]] | |||
[[Category: Haim A]] | |||
[[Category: Hennig S]] | |||
[[Category: Klintrot CIR]] | |||
[[Category: Liebscher S]] | |||
[[Category: Neubacher S]] | |||
Latest revision as of 15:55, 1 April 2026
INCYPRO crosslinked dimer of the D-stereospecific hydrolase dHy1
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