3EFU

X-ray structure of human ubiquitin-Hg(II) adduct

Summary for 3EFU

• Entry DOI: 10.2210/pdb3efu/pdb
• Related: 1UBQ
• Descriptor: Ubiquitin, MERCURY (II) ION (3 entities in total)
• Functional Keywords: protein-metal ion complex, ubiquitin, cadmium, adduct, cytoplasm, nucleus, phosphoprotein, ubl conjugation, protein transport
• Biological source: Homo sapiens
• Total number of polymer chains: 1
• Total formula weight: 8777.42

Authors

Falini, G.,Fermani, S.,Tosi, G. (deposition date: 2008-09-10, release date: 2008-12-09, Last modification date: 2023-11-01)

Primary citation

Falini, G.,Fermani, S.,Tosi, G.,Arnesano, F.,Natile, G.
Structural probing of Zn(ii), Cd(ii) and Hg(ii) binding to human ubiquitin.
Chem.Commun.(Camb.), 45:5960-5962, 2008

PubMed Abstract: A structural investigation performed on adducts of human ubiquitin with group-12 metal ions reveals common preferential anchoring sites, the most populated one being His68; at higher metal ion concentration a second and a third site, close to the N-terminus of the protein, become populated and promote a polymorphic transition from orthorhombic to cubic form; Glu16 and Glu18, involved in the latter metal binding, undergo a remarkable displacement from their position in native ubiquitin; the aggregate stereochemistry appears to be driven by the clustering of deshielded backbone hydrogen-bond patches, and metal ions foster this process.

PubMed: 19030552
DOI: 10.1039/b813463d

Experimental method

X-RAY DIFFRACTION (1.84 Å)