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Issue 6, 1997
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Structural model of rabbit liver copper metallothionein


Molecular modelling techniques have been used to calculate the structure for the primary, mammalian copper-containing protein, metallothionein Cu 12 -MT. Structural information obtained from existing spectroscopic data and comparison with inorganic copper(I)–thiolate model compounds were employed. A two-domain structure, with stoichiometries of Cu 6 S 9 and Cu 6 S 11 , was constructed in which the copper(I)–cysteine connections were based on the arrangement of the cysteines in the Zn 7 -MT precursor as determined by previous 1 H NMR studies. In the minimized structure, in which metal–thiolate bond lengths and angles were allowed to vary, each copper(I) was trigonally co-ordinated by cysteine thiolates; the average bond length was calculated to be close to 224 pm. In the α domain of the protein both bridging (7S) and terminal (4S) thiolate ligation take part in the Cu 6 S 11 cluster structure, in the β domain all nine thiolates bridge pairs of Cu I atoms to form the Cu 6 S 9 cluster structure. Significantly, the energy-minimized structure exhibits two main crevices that are similar to those reported for the structure of Cd 5 Zn 2 -MT 1 obtained by analysis of X-ray diffraction data. These crevices could allow access to the otherwise embedded copper–thiolate clusters.

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Article type: Paper
DOI: 10.1039/A605462E
J. Chem. Soc., Dalton Trans., 1997, 977-984

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    Structural model of rabbit liver copper metallothionein

    A. Presta, D. A. Fowle and M. J. Stillman, J. Chem. Soc., Dalton Trans., 1997, 977
    DOI: 10.1039/A605462E

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