2AW0

FOURTH METAL-BINDING DOMAIN OF THE MENKES COPPER-TRANSPORTING ATPASE, NMR, 20 STRUCTURES

Summary for 2AW0

• Entry DOI: 10.2210/pdb2aw0/pdb
• Descriptor: MENKES COPPER-TRANSPORTING ATPASE, SILVER ION (2 entities in total)
• Functional Keywords: copper-transporting atpase, copper-binding domain, hydrolase, copper transport
• Biological source: Homo sapiens (human)
• Cellular location: Golgi apparatus, trans-Golgi network membrane ; Multi-pass membrane protein . Isoform 3: Cytoplasm, cytosol . Isoform 5: Endoplasmic reticulum : Q04656
• Total number of polymer chains: 1
• Total formula weight: 7744.43

Authors

Gitschier, J.,Fairbrother, W.J. (deposition date: 1997-10-08, release date: 1998-01-14, Last modification date: 2024-05-01)

Primary citation

Gitschier, J.,Moffat, B.,Reilly, D.,Wood, W.I.,Fairbrother, W.J.
Solution structure of the fourth metal-binding domain from the Menkes copper-transporting ATPase.
Nat.Struct.Biol., 5:47-54, 1998

PubMed Abstract: Menkes disease is an X-linked disorder in copper transport that results in death during early childhood. The solution structures of both apo and Ag(I)-bound forms of the fourth metal-binding domain (mbd4) from the Menkes copper-transporting ATPase have been solved. The 72-residue mbd4 has a ferredoxin-like beta alpha beta beta alpha beta fold. Structural differences between the two forms are limited to the metal-binding loop, which is disordered in the apo structure but well ordered in the Ag(I)-bound structure. Ag(I) binds in a linear bicoordinate manner to the two Cys residues of the conserved GMTCxxC motif; Cu(I) likely coordinates in a similar manner. Menkes mbd4 is thus the first bicoordinate copper-binding protein to be characterized structurally. Sequence comparisons with other heavy-metal-binding domains reveal a conserved hydrophobic core and metal-binding motif.

PubMed: 9437429
DOI: 10.1038/nsb0198-47

Experimental method

SOLUTION NMR