1s6o
From Proteopedia
Solution structure and backbone dynamics of the apo-form of the second metal-binding domain of the Menkes protein ATP7A
Overview
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.
About this Structure
1S6O is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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, Biochemistry. 2004 Mar 30;43(12):3396-403. PMID:15035611 Page seeded by OCA on Sun Apr 13 08:10:40 2008
