Download MendeleyStructural Characterization of the Complex between Hen Egg-White Lysozyme and Zr(IV) -Substituted Keggin Polyoxometalate as Artificial Protease.
Sap, A., De Zitter, E., Van Meervelt, L., Parac-Vogt, T.N.(2015) Chemistry 21: 11692-11695
- PubMed: 26179600
- DOI: https://doi.org/10.1002/chem.201501998
- Primary Citation of Related Structures:
4XYY - PubMed Abstract:
Successful co-crystallization of a noncovalent complex between hen egg-white lysozyme (HEWL) and the monomeric Zr(IV) -substituted Keggin polyoxometalate (POM) (Zr1?K1), (Et2 NH2)3 [Zr(PW11 O39)] (1), has been achieved, and its single-crystal X-ray structure has been determined. The dimeric Zr(IV) -substituted Keggin-type polyoxometalate (Zr1?K2), (Et2 NH2)10 [Zr(PW11 O39 )2] (2), has been previously shown to exhibit remarkable selectivity towards HEWL hydrolysis. The reported X-ray structure shows that the hydrolytically active Zr(IV) -substituted Keggin POM exists as a monomeric species. Prior to hydrolysis, this monomer interacts with HEWL in the vicinity of the previously identified cleavage sites found at Trp28-Val29 and Asn44-Arg45, through water-mediated H-bonding and electrostatic interactions. Three binding sites are observed at the interface of the negatively charged Keggin POM and the positively charged regions of HEWL at: 1)?Gly16, Tyr20, and Arg21; 2)?Asn44, Arg45, and Asn46; and 3)?Arg128.
Organizational Affiliation:
Department of Chemistry, KU Leuven, Celestijnenlaan 200F box 2404, 3001 Leuven, Heverlee (Belgium).
