2GQK

Solution structure of Human Ni(II)-Sco1


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 350 
  • Conformers Submitted: 30 
  • Selection Criteria: target function 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

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.

(2006) Proc Natl Acad Sci U S A 103: 8595-8600

  • DOI: https://doi.org/10.1073/pnas.0601375103
  • Primary Citation of Related Structures:  
    2GGT, 2GQK, 2GQL, 2GQM, 2GT5, 2GT6, 2GVP

  • 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.


  • Organizational Affiliation

    Magnetic Resonance Center and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019 Florence, Italy.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
SCO1 protein homolog, mitochondrial173Homo sapiensMutation(s): 0 
Gene Names: SCO1SCOD1
UniProt & NIH Common Fund Data Resources
Find proteins for O75880 (Homo sapiens)
Explore O75880 
Go to UniProtKB:  O75880
PHAROS:  O75880
GTEx:  ENSG00000133028 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO75880
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
NI
Query on NI

Download Ideal Coordinates CCD File 
B [auth A]NICKEL (II) ION
Ni
VEQPNABPJHWNSG-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 350 
  • Conformers Submitted: 30 
  • Selection Criteria: target function 

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2006-06-06
    Type: Initial release
  • Version 1.1: 2008-05-01
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2022-03-09
    Changes: Data collection, Database references, Derived calculations