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• W4240328963 abstract "Abstract The first structure of yeast copper metallothionein (1) was determined from solution NMR data using experimental NOEs and dihedral angle constraints along with specific metal to Cys connectivities derived for the isomorphic Ag(I) substituted Cu(I) yeast MT. In solution, both MTs bind seven moles of Cu(I) or Ag(I) ions, respectively, in a single cluster embedded in a cleft between two large parallel protein loops with only the metals on the open side of the cleft exposed to the solvent. It is reassuring to see the precision of the earlier solution structure compared to the recently published crystal structure (2) of a yeast copper thionein construct lacking the first 4 and last 13 residues of the intact protein. All of the crystal metal–Cys connectivities are identical to the previous solution structure, with the additional verification of the earlier postulated third Cys ligand to metal VI. The only difference is that the truncated, crystallized CuMT protein binds an eighth Cu(I) ion, labeled Cu39. (Note error in (2) where the “copper ion missing in solution structure” is misidentified as Cu44). Considering the fact that two of the three coordinating cysteines for Cu39 in (2) come from the N terminus, it is conceivable that cutting off four residues from this end enables an eighth metal to bind. Unfortunately, no solution study of the Cu(I) binding stoichiometry to this truncated form of the protein was reported. Naturally, the important structure is the structure of the native, full‐length yeast MT. We, therefore, recommend that caution be exercised before drawing any conclusions about the native protein structure on the basis of the crystal structure on the truncated yeast MT construct." @default.
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• W4240328963 date "2004-03-05" @default.
• W4240328963 modified "2023-09-23" @default.
• W4240328963 title "Yeast Copper Metallothionein" @default.
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• W4240328963 doi "https://doi.org/10.1002/0470028637.met203" @default.
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