1S6O: Solution structure and backbone dynamics of the apo-form of the second metal-binding domain of the Menkes protein ATP7A

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.
PDB ID: 1S6ODownload
MMDB ID: 27019
PDB Deposition Date: 2004/1/26
Updated in MMDB: 2007/11
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Molecular Components in 1S6O
Label Count Molecule
Protein (1 molecule)
Copper-transporting Atpase 1(Gene symbol: ATP7A)
Molecule annotation
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Citing MMDB