5L4R

X-ray structure of the adduct between thaumatin and cisplatin

Summary for 5L4R

• Entry DOI: 10.2210/pdb5l4r/pdb
• Descriptor: Thaumatin-1, L(+)-TARTARIC ACID, bis(azanyl)-chloranyl-oxidanyl-platinum, ... (6 entities in total)
• Functional Keywords: cisplatin, drug, model protein, plant protein
• Biological source: Thaumatococcus daniellii (Katemfe)
• Cellular location: Cytoplasmic vesicle: P02883
• Total number of polymer chains: 1
• Total formula weight: 25858.44

Authors

Russo Krauss, I.,Ferraro, G.,Merlino, A. (deposition date: 2016-05-26, release date: 2016-12-07, Last modification date: 2024-11-06)

Primary citation

Russo Krauss, I.,Ferraro, G.,Merlino, A.
Cisplatin-Protein Interactions: Unexpected Drug Binding to N-Terminal Amine and Lysine Side Chains.
Inorg.Chem., 55:7814-7816, 2016

PubMed Abstract: Literature studies carried out by mass spectrometry and X-ray crystallography have demonstrated that cisplatin is able to bind proteins mainly close to Met, His, and free Cys side chains. To identify possible alternative modes of cisplatin binding to proteins at the molecular level, here we have solved the high-resolution X-ray structure of the adduct formed in the reaction between the drug and the model protein thaumatin, which does not contain any His and free Cys residues and possesses just one buried Met. Our data reveal unexpected cisplatin binding sites on the protein surface that could have general significance: cisplatin fragments -[Pt(NH3)2Cl](+), -[Pt(NH3)Cl2], and -[Pt(NH3)2(OH2)](2+) bind to a protein N-terminus and close to Lys and Glu side chains.

PubMed: 27482735
DOI: 10.1021/acs.inorgchem.6b01234

Experimental method

X-RAY DIFFRACTION (1.45 Å)