1M0J
solution structure of the beta domain of mt_nc
Summary for 1M0J
Entry DOI | 10.2210/pdb1m0j/pdb |
Related | 1M0G |
Descriptor | metallothionein MT_nc, CADMIUM ION (2 entities in total) |
Functional Keywords | cadmium thiolate-cluster, metal binding protein |
Biological source | Notothenia coriiceps (yellowbelly rockcod) |
Total number of polymer chains | 1 |
Total formula weight | 3150.45 |
Authors | Capasso, C.,Carginale, V.,Crescenzi, O.,Di Maro, D.,Parisi, E.,Spadaccini, R.,Temussi, P.A. (deposition date: 2002-06-13, release date: 2003-05-06, Last modification date: 2024-05-29) |
Primary citation | Capasso, C.,Carginale, V.,Crescenzi, O.,Di Maro, D.,Parisi, E.,Spadaccini, R.,Temussi, P.A. Solution Structure of MT_nc, a Novel Metallothionein from the Antarctic Fish Notothenia coriiceps. Structure, 11:435-443, 2003 Cited by PubMed 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. PubMed: 12679021DOI: 10.1016/S0969-2126(03)00044-3 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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