1S6O

Solution structure and backbone dynamics of the apo-form of the second metal-binding domain of the Menkes protein ATP7A


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 200 
  • Conformers Submitted: 30 
  • Selection Criteria: target function 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Solution Structure and Backbone Dynamics of the Cu(I) and Apo Forms of the Second Metal-Binding Domain of the Menkes Protein ATP7A.

Banci, L.Bertini, I.Del Conte, R.D'Onofrio, M.Rosato, A.

(2004) Biochemistry 43: 3396-3403

  • DOI: https://doi.org/10.1021/bi036042s
  • Primary Citation of Related Structures:  
    1S6O, 1S6U

  • PubMed Abstract: 

    The second domain of the human Menkes protein (MNK2), formed by 72 residues, has been expressed in Escherichia coli, and its structure has been determined by NMR in both the apo and copper-loaded forms. The structures, obtained with (13)C- and (15)N-labeled samples, are of high quality with backbone rmsd values of 0.51 and 0.41 A and CYANA target functions of 0.39 and 0.38 A(2), respectively. The loop involved in copper binding is part of a hydrophobic patch, which is maintained in both forms. Conformational mobility is observed in the apo form in the same loop. A comparison with metallochaperones and soluble domains of P-type ATPases allows us to relate the primary structure to the occurrence of structural rearrangements upon copper binding.


  • Organizational Affiliation

    Magnetic Resonance Center, University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Copper-transporting ATPase 176Homo sapiensMutation(s): 0 
Gene Names: ATP7AMNKMC1
EC: 3.6.3.4
UniProt & NIH Common Fund Data Resources
Find proteins for Q04656 (Homo sapiens)
Explore Q04656 
Go to UniProtKB:  Q04656
PHAROS:  Q04656
GTEx:  ENSG00000165240 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ04656
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 200 
  • Conformers Submitted: 30 
  • Selection Criteria: target function 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2004-04-06
    Type: Initial release
  • Version 1.1: 2008-04-29
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2022-03-02
    Changes: Database references, Derived calculations
  • Version 1.4: 2024-05-22
    Changes: Data collection