7VIS

Crystal structure of Au(200EQ)-apo-R168H/L169C-rHLFr

7VIS の概要

• エントリーDOI: 10.2210/pdb7vis/pdb
• 分子名称: Ferritin light chain, 1,2-ETHANEDIOL, GOLD ION, ... (7 entities in total)
• 機能のキーワード: ferritin, metal binding protein
• 由来する生物種: Equus caballus (Horse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21788.40

構造登録者

Lu, C.,Peng, X.,Maity, B.,Ito, N.,Abe, S.,Ueno, T.,Lu, D. (登録日: 2021-09-27, 公開日: 2022-06-08, 最終更新日: 2023-11-29)

主引用文献

Lu, C.,Maity, B.,Peng, X.,Ito, N.,Abe, S.,Sheng, X.,Ueno, T.,Lu, D.
Design of a gold clustering site in an engineered apo-ferritin cage.
Commun Chem, 5:39-39, 2022

PubMed Abstract: Water-soluble and biocompatible protein-protected gold nanoclusters (Au NCs) hold great promise for numerous applications. However, design and precise regulation of their structure at an atomic level remain challenging. Herein, we have engineered and constructed a gold clustering site at the 4-fold symmetric axis channel of the apo-ferritin cage. Using a series of X-ray crystal structures, we evaluated the stepwise accumulation process of Au ions into the cage and the formation of a multinuclear Au cluster in our designed cavity. We also disclosed the role of key residues in the metal accumulation process. X-ray crystal structures in combination with quantum chemical (QC) calculation revealed a unique Au clustering site with up to 12 Au atoms positions in the cavity. Moreover, the structure of the gold nanocluster was precisely tuned by the dosage of the Au precursor. As the gold concentration increases, the number of Au atoms position at the clustering site increases from 8 to 12, and a structural rearrangement was observed at a higher Au concentration. Furthermore, the binding affinity order of the four Au binding sites on apo-ferritin was unveiled with a stepwise increase of Au precursor concentration.

PubMed: 36697940
DOI: 10.1038/s42004-022-00651-1

実験手法

X-RAY DIFFRACTION (1.85 Å)