2gql
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Solution structure of Human Ni(II)-Sco1
OverviewOverview
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.
DiseaseDisease
Known diseases associated with this structure: Hepatic failure, early onset, and neurologic disorder OMIM:[603644]
About this StructureAbout this Structure
2GQL is a Single protein structure of sequence from Homo sapiens with NI as ligand. Full crystallographic information is available from OCA.
ReferenceReference
A hint for the function of human Sco1 from different structures., Banci L, Bertini I, Calderone V, Ciofi-Baffoni S, Mangani S, Martinelli M, Palumaa P, Wang S, Proc Natl Acad Sci U S A. 2006 Jun 6;103(23):8595-600. Epub 2006 May 30. PMID:16735468
Page seeded by OCA on Mon Nov 12 22:21:18 2007