Structural highlights
Function
MTA_NOTNE Metallothioneins have a high content of cysteine residues that bind various heavy metals.
Publication Abstract from PubMed
The structure of [113Cd(7)]-metallothionein (MT_nc) of the Antarctic fish Notothenia coriiceps, the first three-dimensional structure of a fish metallothionein, was determined by homonuclear 1H NMR experiments and heteronuclear [1H, 113Cd]-correlation spectroscopy. MT_nc is composed of an N-terminal beta domain with 9 cysteines and 3 metal ions and a carboxy-terminal alpha-domain with 11 cysteines and 4 metal ions. The position of the ninth Cys of the alpha domain of MT_nc is different from the corresponding Cys of mammalian MTs. As a result, the last CXCC motif in the mammalian MT sequence becomes CXXXCC in the fish MT. This difference leads to a structural change of the alpha domain and, in turn, to a different charge distribution with respect to that observed in mammalian metallothioneins.
Solution structure of MT_nc, a novel metallothionein from the Antarctic fish Notothenia coriiceps.,Capasso C, Carginale V, Crescenzi O, Di Maro D, Parisi E, Spadaccini R, Temussi PA Structure. 2003 Apr;11(4):435-43. PMID:12679021[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Capasso C, Carginale V, Crescenzi O, Di Maro D, Parisi E, Spadaccini R, Temussi PA. Solution structure of MT_nc, a novel metallothionein from the Antarctic fish Notothenia coriiceps. Structure. 2003 Apr;11(4):435-43. PMID:12679021
