9T0V

Crystal structure of H416C NikA mutant from Escherichia coli in complex with Fe(III)-EDTA

Summary for 9T0V

• Entry DOI: 10.2210/pdb9t0v/pdb
• Descriptor: Nickel-binding periplasmic protein, FE (III) ION, {[-(BIS-CARBOXYMETHYL-AMINO)-ETHYL]-CARBOXYMETHYL-AMINO}-ACETIC ACID, ... (8 entities in total)
• Functional Keywords: nickel importer fe(iii)-edta binding his416cys mutation, metal binding protein
• Biological source: Escherichia coli K-12
• Total number of polymer chains: 2
• Total formula weight: 113873.52

Authors

Cavazza, C.,Menage, S. (deposition date: 2025-10-20, release date: 2026-06-10)

Primary citation

Boukhallat, M.,Benhamed, I.,Arnone, J.,Van Baaren, S.,Rinaldi, C.,Catty, P.,Marchi-Delapierre, C.,Cavazza, C.,Menage, S.
Covalent Insertion of a Mn(Salen) Type Complex in Cross-Linked Protein Crystals: Design of an Enantioselective Artificial Epoxidase.
Chemistry, :e71159-e71159, 2026

PubMed Abstract: Artificial enzymes represent a promising alternative for performing non-natural reactions in biocatalysis. Here, we illustrate the potential of cross-linked enzyme crystals (CLEC) to achieve enantioselective epoxidation through the generation of an artificial enzyme obtained by direct covalent anchoring of a manganese complex as an artificial active site within a protein. Enantiomeric excess (ee) of up to 90% on cis-β-methylstyrene was measured when the covalent binding yield was maximized, thanks to the remarkable behavior of the crystals. The structure of the modified enzyme, NikA, is provided. This work adds to the growing body of examples highlighting the advantages of CLEC in oxidation catalysis.

PubMed: 42210913
DOI: 10.1002/chem.71159

Experimental method

X-RAY DIFFRACTION (2.542 Å)