8fts
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==SgvM methyltransferase with SAH and alpha-ketoleucine== | |
| + | <StructureSection load='8fts' size='340' side='right'caption='[[8fts]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8fts]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_griseoviridis Streptomyces griseoviridis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8FTS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8FTS 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]] 2.2Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COI:2-OXO-4-METHYLPENTANOIC+ACID'>COI</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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=8fts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8fts OCA], [https://pdbe.org/8fts PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8fts RCSB], [https://www.ebi.ac.uk/pdbsum/8fts PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8fts ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/R9UTR3_STRGD R9UTR3_STRGD] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Catalytic asymmetric alpha-alkylation of carbonyl compounds represents a long-standing challenge in synthetic organic chemistry. Herein, we advance a dual biocatalytic platform for the efficient asymmetric alkylation of alpha-keto acids. First, guided by our recently obtained crystal structures, we develop SgvM(VAV) as a general biocatalyst for the enantioselective methylation, ethylation, allylation and propargylation of a range of alpha-keto acids with total turnover numbers (TTNs) up to 4,600. Second, we mine a family of bacterial HMTs from Pseudomonas species sharing less than 50% sequence identities with known HMTs and evaluated their activities in SAM regeneration. Our best performing HMT from P. aeruginosa, PaHMT, displays the highest SAM regeneration efficiencies (TTN up to 7,700) among HMTs characterized to date. Together, the synergistic use of SgvM(VAV) and PaHMT affords a fully biocatalytic protocol for asymmetric methylation featuring a record turnover efficiency, providing a solution to the notorious problem of asymmetric alkylation. | ||
| - | + | A biocatalytic platform for asymmetric alkylation of alpha-keto acids by mining and engineering of methyltransferases.,Ju S, Kuzelka KP, Guo R, Krohn-Hansen B, Wu J, Nair SK, Yang Y Nat Commun. 2023 Sep 14;14(1):5704. doi: 10.1038/s41467-023-40980-w. PMID:37709735<ref>PMID:37709735</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Kuzelka | + | <div class="pdbe-citations 8fts" style="background-color:#fffaf0;"></div> |
| - | [[Category: Nair | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Streptomyces griseoviridis]] | ||
| + | [[Category: Kuzelka K]] | ||
| + | [[Category: Nair SK]] | ||
Current revision
SgvM methyltransferase with SAH and alpha-ketoleucine
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