1s6o

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1s6o

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

Contents

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.

Disease

Known diseases associated with this structure: Analgesia from kappa-opioid receptor agonist, female-specific OMIM:[155555], Blond/light brown hair and/or fair skin OMIM:[155555], Cutis laxa, neonatal OMIM:[300011], Melanoma, susceptiblity to OMIM:[155555], Menkes disease OMIM:[300011], Occipital horn syndrome OMIM:[300011], Oculocutaneous albinism, type II, modifier of OMIM:[155555], Red hair/fair skin OMIM:[155555], UV-induced skin damage, susceptibility to OMIM:[155555]

About this Structure

1S6O is a Single protein structure of sequence from Homo sapiens. Active as Copper-exporting ATPase, with EC number 3.6.3.4 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

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