AI Article Synopsis
- The first three-dimensional structure of metallothionein from the Antarctic fish Notothenia coriiceps was revealed through advanced NMR techniques.
- The metallothionein consists of two domains: 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.
- A key structural difference was found in the alpha domain's ninth cysteine position compared to mammalian metallothioneins, resulting in a unique charge distribution in the fish protein.
Article Abstract
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.
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| http://dx.doi.org/10.1016/s0969-2126(03)00044-3 | DOI Listing |
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