24ci: Difference between revisions
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==Crystal structure of MonCI mutant Q441W== | |||
<StructureSection load='24ci' size='340' side='right'caption='[[24ci]], [[Resolution|resolution]] 2.75Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[24ci]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_virginiae Streptomyces virginiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=24CI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=24CI 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]] 2.751Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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=24ci FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=24ci OCA], [https://pdbe.org/24ci PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=24ci RCSB], [https://www.ebi.ac.uk/pdbsum/24ci PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=24ci ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q846W9_STRVG Q846W9_STRVG] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Improving enzyme stability without compromising catalytic activity remains a major challenge in protein engineering. Here, we present a co-evolution-guided strategy to enhance both thermostability and catalytic performance of the flavin-dependent monooxygenase MonCI, an enzyme involved in monensin biosynthesis. By combining sequence covariation analysis with structural filtering, a focused library of 15 single mutants yielded 4 variants with increased stability and activity. Combinatorial assembly generated triple, quadruple and quintuple mutants, with the best-performing quadruple variants exhibiting up to a 10 degrees C increase in melting temperature, a 2.3-fold increase in specific activity, and a 2.1-fold longer half-life, accompanied by enhanced turnover despite reduced substrate affinity. Crystal structures and molecular dynamics simulations reveal that stabilization arises from strengthened intramolecular networks of hydrogen bonds, salt bridges, and hydrophobic interactions, while epistatic effects limit additive improvements. This work provides mechanistic insight into how co-evolving residues modulate enzyme structure and function, presents a useful co-evolution-guided strategy for enzyme design, and advances MonCI as a promising biocatalyst for asymmetric epoxidation. | |||
Co-evolution-guided engineering of monensin biosynthetic monooxygenase MonCI reveals mechanistic basis for concurrent stability and catalytic enhancement.,Xiao H, Li J, Zhou J, Liu C, Deng Y, Wang S, Tong Z, Liu J, Zheng Z, Zhong J, Li H, Chen X Int J Biol Macromol. 2026 Aug 20;381(Pt 1):154119. doi: , 10.1016/j.ijbiomac.2026.154119. PMID:42624264<ref>PMID:42624264</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 24ci" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Streptomyces virginiae]] | |||
[[Category: Chen X]] | |||
[[Category: Xiao HL]] | |||
Latest revision as of 16:40, 8 September 2026
Crystal structure of MonCI mutant Q441W
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