2GGT

Crystal structure of human SCO1 complexed with nickel.

Summary for 2GGT

• Entry DOI: 10.2210/pdb2ggt/pdb
• Related: 1on4 1wp0
• Descriptor: SCO1 protein homolog, mitochondrial, NICKEL (II) ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: copper chaperone, cu-binding protein, mitochondrial assembly factor, redox, nickel, disuplhide, mitochondrion, chaperone
• Biological source: Homo sapiens (human)
• Cellular location: Mitochondrion: O75880
• Total number of polymer chains: 2
• Total formula weight: 37684.56

Authors

Banci, L.,Bertini, I.,Calderone, V.,Ciofi-Baffoni, S.,Mangani, S.,Martinelli, M.,Palumaa, P.,Wang, S. (deposition date: 2006-03-24, release date: 2006-05-16, Last modification date: 2024-11-13)

Primary citation

Banci, L.,Bertini, I.,Calderone, V.,Ciofi-Baffoni, S.,Mangani, S.,Martinelli, M.,Palumaa, P.,Wang, S.
A hint for the function of human Sco1 from different structures.
Proc.Natl.Acad.Sci.Usa, 103:8595-8600, 2006

PubMed Abstract: The solution structures of apo, Cu(I), and Ni(II) human Sco1 have been determined. The protein passes from an open and conformationally mobile state to a closed and rigid conformation upon metal binding as shown by electrospray ionization MS and NMR data. The metal ligands of Cu(I) are two Cys residues of the CPXXCP motif and a His residue. The latter is suitably located to coordinate the metal anchored by the two Cys residues. The coordination sphere of Ni(II) in solution is completed by another ligand, possibly Asp. Crystals of the Ni(II) derivative were also obtained with the Ni(II) ion bound to the same His residue and to the two oxidized Cys residues of the CPXXCP motif. We propose that the various structures solved here represent the various states of the protein in its functional cycle and that the metal can be bound to the oxidized protein at a certain stage. Although it now seems reasonable that Sco1, which is characterized by a thioredoxin fold, has evolved to bind a metal atom via the di-Cys motif to act as a copper chaperone, the oxidized form of the nickel-bound protein suggests that it may also maintain the thioredoxin function.

PubMed: 16735468
DOI: 10.1073/pnas.0601375103

Experimental method

X-RAY DIFFRACTION (2.4 Å)