6jsu: Difference between revisions
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<StructureSection load='6jsu' size='340' side='right'caption='[[6jsu]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='6jsu' size='340' side='right'caption='[[6jsu]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6jsu]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6jsu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_kaustophilus_HTA426 Geobacillus kaustophilus HTA426]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JSU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JSU FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6jsu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jsu OCA], [https://pdbe.org/6jsu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jsu RCSB], [https://www.ebi.ac.uk/pdbsum/6jsu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jsu ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5KZU5_GEOKA Q5KZU5_GEOKA] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 6jsu" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6jsu" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Phosphotriesterase 3D structures|Phosphotriesterase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Geobacillus kaustophilus HTA426]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Xue | [[Category: Xue B]] | ||
[[Category: Yew | [[Category: Yew WS]] | ||
Latest revision as of 13:19, 22 November 2023
Structure of Geobacillus kaustophilus lactonase, Y99C/D266N double mutantStructure of Geobacillus kaustophilus lactonase, Y99C/D266N double mutant
Structural highlights
FunctionPublication Abstract from PubMedIn this work, we present a generalizable directed computational evolution protocol to effectively reduce the sequence space to be explored in rational enzyme design. The protocol involves in silico mutation modeling and substrate docking to rapidly identify mutagenesis hotspots that may enhance an enzyme's substrate binding and overall catalysis. By applying this protocol to a quorum-quenching Geobacillus kaustophilus lactonase, GKL, we generated 1,881 single mutants and docked high-energy intermediates of nine acyl homoserine lactones onto them. We found that Phe28 and Tyr99 were two hotspots that produced most of the predicted top 20 mutants. Of the 180 enzyme-substrate combinations (top 20 mutants x 9 substrates), 51 (28%) exhibited enhanced substrate binding and 22 (12%) had better overall activity when compared with wild-type GKL. X-ray crystallographic studies of Y99C and Y99P provided rationalized explanations for the enhancement in enzyme function and corroborated the utility of the protocol. Directed Computational Evolution of Quorum-Quenching Lactonases from the Amidohydrolase Superfamily.,Go MK, Zhao LN, Xue B, Supekar S, Robinson RC, Fan H, Yew WS Structure. 2020 Apr 6. pii: S0969-2126(20)30093-9. doi:, 10.1016/j.str.2020.03.011. PMID:32320671[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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