7ZC3

Crystal structure of human copper chaperone Atox1 bound to zinc ion by CxxC motif

Summary for 7ZC3

• Entry DOI: 10.2210/pdb7zc3/pdb
• Descriptor: Copper transport protein ATOX1, ZINC ION, SULFATE ION, ... (4 entities in total)
• Functional Keywords: copper transport protein, metallochaperone, atox1 protein, metal ions, zinc, chaperone
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 15467.08

Authors

Mangini, V.,Belviso, B.D.,Arnesano, F.,Caliandro, R. (deposition date: 2022-03-25, release date: 2022-04-06, Last modification date: 2024-01-31)

Primary citation

Mangini, V.,Belviso, B.D.,Nardella, M.I.,Natile, G.,Arnesano, F.,Caliandro, R.
Crystal Structure of the Human Copper Chaperone ATOX1 Bound to Zinc Ion.
Biomolecules, 12:-, 2022

PubMed Abstract: 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.

PubMed: 36291703
DOI: 10.3390/biom12101494

Experimental method

X-RAY DIFFRACTION (1.9 Å)