6ZS8

X-ray structure of the adduct formed upon treating lysozyme with an aged solution of arsenoplatin-1

This is a non-PDB format compatible entry.

Summary for 6ZS8

• Entry DOI: 10.2210/pdb6zs8/pdb
• Descriptor: Lysozyme, NITRATE ION, 1,2-ETHANEDIOL, ... (7 entities in total)
• Functional Keywords: platinum, aresenic, bimetallin, protein binding, aggregation, hydrolase
• Biological source: Gallus gallus (Chicken)
• Total number of polymer chains: 1
• Total formula weight: 17669.19

Authors

Ferraro, G.,Merlino, A. (deposition date: 2020-07-15, release date: 2020-12-23, Last modification date: 2024-11-06)

Primary citation

Ferraro, G.,Cirri, D.,Marzo, T.,Pratesi, A.,Messori, L.,Merlino, A.
The first step of arsenoplatin-1 aggregation in solution unveiled by solving the crystal structure of its protein adduct.
Dalton Trans, 50:68-71, 2021

PubMed Abstract: Arsenoplatin-1 (AP-1) is an innovative dual-action anticancer agent that contains a platinum(ii) center coordinated to an arsenous acid moiety. We found that AP-1 spontaneously aggregates in aqueous solutions generating oligomeric species of increasing length. Afterward, we succeeded in solving the crystal structure of the adduct formed between the model protein lysozyme and an early AP-1 oligomer that turned out to be a trimer. Remarkably, this crystal structure traps an early stage of AP-1 aggregation offering detailed insight into the molecular process of the oligomer's growth.

PubMed: 33320144
DOI: 10.1039/d0dt04068a

Experimental method

X-RAY DIFFRACTION (2.153 Å)