Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7VIO

Crystal structure of recombinant horse spleen apo-R168H/L169C-Fr

Summary for 7VIO
Entry DOI10.2210/pdb7vio/pdb
DescriptorFerritin light chain, GLYCEROL, CADMIUM ION, ... (5 entities in total)
Functional Keywordsferritin, metal binding protein
Biological sourceEquus caballus (Horse)
Total number of polymer chains1
Total formula weight20464.82
Authors
Lu, C.,Peng, X.,Maity, B.,Ito, N.,Abe, S.,Wu, J.,Ueno, T.,Lu, D. (deposition date: 2021-09-27, release date: 2022-06-08, Last modification date: 2023-11-29)
Primary citationLu, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.5 Å)
Structure validation

226707

數據於2024-10-30公開中

PDB statisticsPDBj update infoContact PDBjnumon