4.7 Article

Crystal Structure of the Human Copper Chaperone ATOX1 Bound to Zinc Ion

期刊

BIOMOLECULES
卷 12, 期 10, 页码 -

出版社

MDPI
DOI: 10.3390/biom12101494

关键词

X-ray crystallography; molecular structure; metal ions; zinc; copper transport proteins; metallochaperones; Atox1

资金

  1. Italian Ministero dell'Universita e della Ricerca [PRIN 2017WBZFHL]

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The bioavailability of copper in human cells may be influenced by the presence of zinc ions. This study demonstrates that zinc ions can target the Cu-chaperone Atox1 and deliver it to Cu-transporting ATPases. The crystal structure of Atox1 loaded with zinc confirms the presence and location of the zinc ion. These findings suggest a potential interplay between Cu and Zn transport mechanisms in human cells.
The bioavailability of copper (Cu) in human cells may depend on a complex interplay with zinc (Zn) ions. We investigated the ability of the Zn ion to target the human Cu-chaperone Atox1, a small cytosolic protein capable of anchoring Cu(I), by a conserved surface-exposed Cys-X-X-Cys (CXXC) motif, and deliver it to Cu-transporting ATPases in the trans-Golgi network. The crystal structure of Atox1 loaded with Zn displays the metal ion bridging the CXXC motifs of two Atox1 molecules in a homodimer. The identity and location of the Zn ion were confirmed through the anomalous scattering of the metal by collecting X-ray diffraction data near the Zn K-edge. Furthermore, soaking experiments of the Zn-loaded Atox1 crystals with a strong chelating agent, such as EDTA, caused only limited removal of the metal ion from the tetrahedral coordination cage, suggesting a potential role of Atox1 in Zn metabolism and, more generally, that Cu and Zn transport mechanisms could be interlocked in human cells.

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