9HRU

The Lysozyme - pctx complex in space group P3121

This is a non-PDB format compatible entry.

Summary for 9HRU

• Entry DOI: 10.2210/pdb9hru/pdb
• Descriptor: Lysozyme C, phosphated-cyclotrixylohydroquinoylene, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (5 entities in total)
• Functional Keywords: complex, hydrolase
• Biological source: Gallus gallus (chicken)
• Total number of polymer chains: 2
• Total formula weight: 30706.77

Authors

Wren, C.P.,Flood, R.J.,Crowley, P.B. (deposition date: 2024-12-18, release date: 2025-08-20)

Primary citation

Wren, C.P.,Flood, R.J.,Mockler, N.M.,Savko, M.,Malinska, M.,Shi, Q.,Crowley, P.B.
Protein Recognition and Assembly by a Phosphocavitand.
J.Am.Chem.Soc., 147:28107-28116, 2025

PubMed Abstract: Controlled protein assembly is an enabling technology, in particular, for biomaterials fabrication. Here, we report protein recognition and assembly by a phosphate-containing macrocycle (). We show that the -symmetric phosphocavitand is a versatile receptor for N-terminal residues or arginine but not lysine. Using atomic resolution X-ray diffraction data, we reveal the precise details of N-terminal complexation in the β-propeller protein lectin (RSL). In some cocrystal structures, a tetrahedral cluster of the phosphocavitand occupies one end of the β-propeller fold, providing a node for protein assembly. The macrocycle cluster is compatible with different types of precipitants, a broad pH range, and zinc complexation. We demonstrate system control with an arginine-enriched RSL that alters the overall assembly due to selective arginine complexation by . A lysozyme- cocrystal structure also demonstrates arginine complexation by the macrocycle. An alternative macrocycle cluster occurs with an engineered RSL bearing an extended N-terminus. In this structure, involving zinc ligation at the N-terminus, the macrocycle forms trimeric clusters and four such clusters form cage-like substructures within the tetrahedral protein framework. Thus, N-terminal complexation in combination with phosphocavitand self-assembly provides new routes to protein crystal engineering.

PubMed: 40694812
DOI: 10.1021/jacs.5c08121

Experimental method

X-RAY DIFFRACTION (1.88 Å)