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8hjx
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of a cupin protein (tm1459, H52A/H58E mutant) in copper (Cu) substituted form== | |
| + | <StructureSection load='8hjx' size='340' side='right'caption='[[8hjx]], [[Resolution|resolution]] 1.15Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8hjx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HJX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HJX FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</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=8hjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hjx OCA], [https://pdbe.org/8hjx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hjx RCSB], [https://www.ebi.ac.uk/pdbsum/8hjx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hjx ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q9X1H0_THEMA Q9X1H0_THEMA] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | We repurposed the metal-binding site of a cupin superfamily protein into the 2-His-1-carboxylate facial triad, which is one of the common motifs in natural non-heme enzymes, to construct artificial metalloenzymes that can catalyze new-to-nature reactions. The Cu(2+)-H52A/H58E variant catalyzed the stereoselective Michael addition reaction and was found to bear a flexible metal-binding site in the high-resolution crystal structure. Furthermore, the H52A/H58E/F104W mutant accommodated a water molecule, which was supported by Glu58 and Trp104 residues via hydrogen bonding, presumably leading to high stereoselectivity. Thus, the 2-His-1-carboxylate facial triad was confirmed to be a versatile and promising metal-binding motif for abiological and canonical biological reactions. | ||
| - | + | An artificial metallolyase with pliable 2-His-1-carboxylate facial triad for stereoselective Michael addition.,Matsumoto R, Yoshioka S, Yuasa M, Morita Y, Kurisu G, Fujieda N Chem Sci. 2023 Mar 13;14(14):3932-3937. doi: 10.1039/d2sc06809e. eCollection 2023 , Apr 5. PMID:37035687<ref>PMID:37035687</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8hjx" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Thermotoga maritima MSB8]] | ||
| + | [[Category: Fujieda N]] | ||
| + | [[Category: Kurisu G]] | ||
| + | [[Category: Matsumoto R]] | ||
Current revision
Crystal structure of a cupin protein (tm1459, H52A/H58E mutant) in copper (Cu) substituted form
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