1S6U

Solution structure and backbone dynamics of the Cu(I) form of the second metal-binding domain of the Menkes protein ATP7A

Summary for 1S6U

• Entry DOI: 10.2210/pdb1s6u/pdb
• Related: 1s6o
• NMR Information: BMRB: 6129
• Descriptor: Copper-transporting ATPase 1, COPPER (I) ION (2 entities in total)
• Functional Keywords: copper homeostasis, metal transport, menkes, structural proteomics in europe, spine, structural genomics, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein. Isoform 3: Cytoplasm, cytosol (Probable). Isoform 5: Endoplasmic reticulum: Q04656
• Total number of polymer chains: 1
• Total formula weight: 8523.53

Authors

Banci, L.,Bertini, I.,Del Conte, R.,D'Onofrio, M.,Rosato, A.,Structural Proteomics in Europe (SPINE) (deposition date: 2004-01-27, release date: 2004-04-06, Last modification date: 2024-05-22)

Primary citation

Banci, L.,Bertini, I.,Del Conte, R.,D'Onofrio, M.,Rosato, A.
Solution Structure and Backbone Dynamics of the Cu(I) and Apo Forms of the Second Metal-Binding Domain of the Menkes Protein ATP7A.
Biochemistry, 43:3396-3403, 2004

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.

PubMed: 15035611
DOI: 10.1021/bi036042s

Experimental method

SOLUTION NMR