Banci Lucia, Bertini Ivano, Cantini Francesca, DellaMalva Nunzia, Herrmann Torsten, Rosato Antonio, Wüthrich Kurt
Magnetic Resonance Center (CERM), University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy.
J Biol Chem. 2006 Sep 29;281(39):29141-7. doi: 10.1074/jbc.M603176200. Epub 2006 Jul 26.
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. MNK3 is 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 beta-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.
人门克斯蛋白（MNK3）的第三个金属结合结构域是一种铜（I）转运ATP酶，已在大肠杆菌中表达并在溶液中进行了表征。研究了MNK3的溶液结构、其与铜（I）的结合特性以及它与生理伴侣HAH1的相互作用。MNK3是门克斯蛋白中结构与其他结构域差异最大的结构域。与其他已知的同源蛋白或蛋白结构域相比，这反映在四链β折叠的最后一条链发生了显著重排。MNK3在与铜（I）离子的相互作用方面也很特殊，因为它被发现是一种相对较弱的结合剂。通过实验观察到了从金属负载的HAH1转移铜（I），但金属分布向HAH1结合方向偏移。这与在门克斯蛋白的其他结构域中观察到的情况不同。
