Solution structure of MT_nc, a novel metallothionein from the Antarctic fish Notothenia coriiceps.
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.
Capasso
Clemente
C
CNR, Institute of Protein Biochemistry, via Marconi 10, I 80125, Naples, Italy.
Carginale
Vincenzo
V
Crescenzi
Orlando
O
Di Maro
Daniela
D
Parisi
Elio
E
Spadaccini
Roberta
R
Temussi
Piero Andrea
PA
D000595:Amino Acid Sequence; D000818:Animals; D000864:Antarctic Regions; D005399:Fishes / Q000378:metabolism*; D008668:Metallothionein / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment
D008668:Metallothionein