9T05

X-ray structure of the adduct formed by dirhodium tetraacetate with a C-phycocyanin

これはPDB形式変換不可エントリーです。

9T05 の概要

• エントリーDOI: 10.2210/pdb9t05/pdb
• 分子名称: C-phycocyanin alpha subunit, C-phycocyanin beta chain, PHYCOCYANOBILIN, ... (6 entities in total)
• 機能のキーワード: dirhodium compounds; paddlewheel dimetallic complexes; metal-protein adducts; metallodrugs; protein metalation, photosynthesis
• 由来する生物種: Galdieria phlegrea; 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 229546.10

構造登録者

Merlino, A.,Ferraro, G. (登録日: 2025-10-16, 公開日: 2025-12-17, 最終更新日: 2025-12-24)

主引用文献

Ferraro, G.,Imbimbo, P.,Troisi, R.,Monti, D.M.,Merlino, A.
Coordination of a Dirhodium(II) Center to Methionine and Cysteine Side Chains: Evidence from X-Ray Structure of the Adduct Formed by Dirhodium Tetraacetate with a C-Phycocyanin.
Int J Mol Sci, 26:-, 2025

PubMed Abstract: Upon reaction of dirhodium tetraacetate ([Rh(μ-OCCH)]) and some [Rh(μ-OCCH)] derivatives with proteins, dimeric Rh-Rh units (diRh) or monometallic moieties can bind the side chains of His, Cys, Met, Asp, Asn, Arg and Lys, and the C-terminal carboxylate. However, structural data on the interaction between the diRh center and Cys and Met side chains within the protein environment are still missing. Here, we report the X-ray structure of the adduct that [Rh(μ-OCCH)] forms with C-phycocyanin from at 2.17 Å resolution. Twelve diRh binding sites were found on the protein structure, two for each (αβ) unit. Dimetallic fragments were observed close to the side chains of Met30 of β-chains and of Cys73 of α-chains. To the best of our knowledge, the results provide the first unambiguous crystallographic observation of the diRh center binding to Met and Cys protein residues. DiRh binding does not alter overall protein structure and stability. This result will help in the design of new dirhodium-based artificial metalloenzymes.

PubMed: 41373647
DOI: 10.3390/ijms262311492

実験手法

X-RAY DIFFRACTION (2.169 Å)