8hjx | pdb_00008hjx

Crystal structure of a cupin protein (tm1459, H52A/H58E mutant) in copper (Cu) substituted form

spinqualitylabelsall models 8hjx, resolution 1.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8hjx is a 2 chain structure with sequence from Thermotoga maritima MSB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.15Å Ligands: CSD, CU Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9X1H0_THEMA 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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