4XYY

Hen Egg-White Lysozyme (HEWL) complexed with Zr(IV)-substituted Keggin-type polyoxometalate

Summary for 4XYY

• Entry DOI: 10.2210/pdb4xyy/pdb
• Descriptor: Lysozyme C, ZIRCONIUM(IV) PHOSPHOTUNGSTATE KEGGIN, DIMETHYL SULFOXIDE, ... (5 entities in total)
• Functional Keywords: co-crystallization, lysozyme, metalsubstituted polyoxometalates, hydrolase
• Biological source: Gallus gallus (Chicken)
• Total number of polymer chains: 1
• Total formula weight: 17298.91

Authors

De Zitter, E.,Van Meervelt, L. (deposition date: 2015-02-03, release date: 2015-07-29, Last modification date: 2024-10-23)

Primary citation

Sap, A.,De Zitter, E.,Van Meervelt, L.,Parac-Vogt, T.N.
Structural Characterization of the Complex between Hen Egg-White Lysozyme and Zr(IV) -Substituted Keggin Polyoxometalate as Artificial Protease.
Chemistry, 21:11692-11695, 2015

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.

PubMed: 26179600
DOI: 10.1002/chem.201501998

Experimental method

X-RAY DIFFRACTION (1.38 Å)