6L2E

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

Summary for 6L2E

• Entry DOI: 10.2210/pdb6l2e/pdb
• Descriptor: Cupin_2 domain-containing protein, COPPER (II) ION, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (4 entities in total)
• Functional Keywords: artificial metalloenzymes, copper enzyme, cupin, metal binding protein
• Biological source: Thermotoga maritima MSB8
• Total number of polymer chains: 2
• Total formula weight: 27170.47

Authors

Fujieda, N.,Ichihashi, H.,Nishikawa, Y.,Kurisu, G.,Itoh, S. (deposition date: 2019-10-03, release date: 2020-04-01, Last modification date: 2023-11-22)

Primary citation

Fujieda, N.,Ichihashi, H.,Yuasa, M.,Nishikawa, Y.,Kurisu, G.,Itoh, S.
Cupin Variants as a Macromolecular Ligand Library for Stereoselective Michael Addition of Nitroalkanes.
Angew.Chem.Int.Ed.Engl., 59:7717-7720, 2020

PubMed Abstract: Cupin superfamily proteins (TM1459) work as a macromolecular ligand framework with a double-stranded β-barrel structure ligating to a Cu ion through histidine side chains. Variegating the first coordination sphere of TM1459 revealed that H52A and H54A/H58A mutants effectively catalyzed the diastereo- and enantioselective Michael addition reaction of nitroalkanes to an α,β-unsaturated ketone. Moreover, calculated substrate docking signified C106N and F104W single-point mutations, which inverted the diastereoselectivity of H52A and further improved the stereoselectivity of H54A/H58A, respectively.

PubMed: 32073197
DOI: 10.1002/anie.202000129

Experimental method

X-RAY DIFFRACTION (1.201 Å)