The third metal-binding domain of the human Menkes protein (MNK3), a copper(I)-transporting ATPase, has been expressed in Escherichia coli and characterized in solution. The solution structure of MNK3, its copper(I)-binding properties, and its interaction with the physiological partner, HAH1, have been studied. MNK3is the domain most dissimilar in structure from the other domains of the Menkes protein. This is reflected in a significant rearrangement of the last strand of the four-stranded β-sheet when compared with the other known homologous proteins or protein domains. MNK3 is also peculiar with respect to its interaction with the copper(I) ion, as it was found to be a comparatively weak binder. Copper(I) transfer from metal-loaded HAH1 was observed experimentally, but the metal distribution was shifted toward binding by HAH1. This is at variance with what is observed for the other Menkes domains. © 2006 by The American Society for Biochemistry and Molecular Biology, Inc.
Solution structure and intermolecular interactions of the third metal-binding domain of ATP7A, the Menkes disease protein / L.Banci; I.Bertini; F.Cantini; N.Della Malva; A.Rosato; T.Herrmann; K.Wuthrich. - In: THE JOURNAL OF BIOLOGICAL CHEMISTRY. - ISSN 0021-9258. - STAMPA. - 281:(2006), pp. 29141-29147. [10.1074/jbc.M603176200]
Solution structure and intermolecular interactions of the third metal-binding domain of ATP7A, the Menkes disease protein
BANCI, LUCIA;BERTINI, IVANO;CANTINI, FRANCESCA;ROSATO, ANTONIO;
2006
Abstract
The third metal-binding domain of the human Menkes protein (MNK3), a copper(I)-transporting ATPase, has been expressed in Escherichia coli and characterized in solution. The solution structure of MNK3, its copper(I)-binding properties, and its interaction with the physiological partner, HAH1, have been studied. MNK3is the domain most dissimilar in structure from the other domains of the Menkes protein. This is reflected in a significant rearrangement of the last strand of the four-stranded β-sheet when compared with the other known homologous proteins or protein domains. MNK3 is also peculiar with respect to its interaction with the copper(I) ion, as it was found to be a comparatively weak binder. Copper(I) transfer from metal-loaded HAH1 was observed experimentally, but the metal distribution was shifted toward binding by HAH1. This is at variance with what is observed for the other Menkes domains. © 2006 by The American Society for Biochemistry and Molecular Biology, Inc.I documenti in FLORE sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.