View source for 8hjy


==Crystal structure of a cupin protein (tm1459, H52A/H58E/F104W mutant) in copper (Cu) substituted form==
<StructureSection load='8hjy' size='340' side='right'caption='[[8hjy]], [[Resolution|resolution]] 1.18&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8hjy]] 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=8HJY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HJY 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]] 1.18&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=8hjy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hjy OCA], [https://pdbe.org/8hjy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hjy RCSB], [https://www.ebi.ac.uk/pdbsum/8hjy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hjy 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8hjy" 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]]