1aw0
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FOURTH METAL-BINDING DOMAIN OF THE MENKES COPPER-TRANSPORTING ATPASE, NMR, 20 STRUCTURES
OverviewOverview
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.
DiseaseDisease
Known diseases associated with this structure: Analgesia from kappa-opioid receptor agonist, female-specific OMIM:[155555], Blond/light brown hair and/or fair skin OMIM:[155555], Cutis laxa, neonatal OMIM:[300011], Melanoma, susceptiblity to OMIM:[155555], Menkes disease OMIM:[300011], Occipital horn syndrome OMIM:[300011], Oculocutaneous albinism, type II, modifier of OMIM:[155555], Red hair/fair skin OMIM:[155555], UV-induced skin damage, susceptibility to OMIM:[155555]
About this StructureAbout this Structure
1AW0 is a Single protein structure of sequence from Homo sapiens. Active as Hydrogen/potassium-exchanging ATPase, with EC number 3.6.3.10 Full crystallographic information is available from OCA.
ReferenceReference
Solution structure of the fourth metal-binding domain from the Menkes copper-transporting ATPase., Gitschier J, Moffat B, Reilly D, Wood WI, Fairbrother WJ, Nat Struct Biol. 1998 Jan;5(1):47-54. PMID:9437429
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