6i8n
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of LmrR with V15 replaced by unnatural amino acid 4-amino-L-phenylalanine== | |
| + | <StructureSection load='6i8n' size='340' side='right' caption='[[6i8n]], [[Resolution|resolution]] 1.79Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6i8n]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6I8N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6I8N FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MPO:3[N-MORPHOLINO]PROPANE+SULFONIC+ACID'>MPO</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HOX:4-AMINO-L-PHENYLALANINE'>HOX</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6i8n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6i8n OCA], [http://pdbe.org/6i8n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6i8n RCSB], [http://www.ebi.ac.uk/pdbsum/6i8n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6i8n ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The impressive rate accelerations that enzymes display in nature often result from boosting the inherent catalytic activities of side chains by their precise positioning inside a protein binding pocket. Here we show that such fine-tuning is also possible for catalytic unnatural amino acids. Specifically, we report the directed evolution of a recently described designer enzyme, which utilizes an aniline side chain to promote a model hydrazone formation reaction. Consecutive rounds of directed evolution identified a number of mutations in the promiscuous binding pocket, in which the unnatural amino acid is embedded in the starting catalyst. When combined, these mutations boost the turnover frequency (kcat) of the designer enzyme by almost 100-fold. Crucially, these gains result from strengthening the catalytic contribution of the unnatural amino acid, as the engineered designer enzymes outperform variants, in which the aniline side chain is replaced with a catalytically inactive tyrosine residue, by >200-fold. | ||
| - | + | Directed evolution of a designer enzyme featuring an unnatural catalytic amino acid.,Mayer C, Dulson C, Reddem E, Thunnissen AM, Roelfes G Angew Chem Int Ed Engl. 2018 Dec 21. doi: 10.1002/anie.201813499. PMID:30575260<ref>PMID:30575260</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6i8n" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Reddem, R]] | ||
| + | [[Category: Thunnissen, A M.W H]] | ||
| + | [[Category: Artificial enzyme]] | ||
| + | [[Category: Dna binding protein]] | ||
| + | [[Category: Engineered variant]] | ||
| + | [[Category: Padr family]] | ||
| + | [[Category: Transcriptional regulator]] | ||
| + | [[Category: Unnatural amino acid]] | ||
Revision as of 06:12, 2 January 2019
Crystal structure of LmrR with V15 replaced by unnatural amino acid 4-amino-L-phenylalanine
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