Comparison of the NMR solution structure and the x-ray crystal structure of rat metallothionein-2.
- 1 November 1992
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 89 (21) , 10124-10128
- https://doi.org/10.1073/pnas.89.21.10124
Abstract
Metallothioneins are small cysteine-rich proteins capable of binding heavy metal ions such as Zn2+ and Cd2+. They are ubiquitous tissue components in higher organisms, which tentatively have been attributed both unspecific protective functions against toxic metal ions and highly specific roles in fundamental zinc-regulated cellular processes. In this paper a detailed comparison of the NMR solution structure [Schultze, P., Wörgötter, E., Braun, W., Wagner, G., Vasák, M., Kägi, J. H. R. & Wüthrich, K. (1988) J. Mol. Biol. 203, 251-268] and a recent x-ray crystal structure [Robbins, A. H., McRee, D. E., Williamson, M., Collett, S. A., Xoung, N. H., Furey, W. F., Wang, B. C. & Stout, C. D. (1991) J. Mol. Biol. 221, 1269-1293] of rat metallothionein-2 shows that the metallothionein structures in crystals and in solution have identical molecular architectures. The structures obtained with both techniques now present a reliable basis for discussions on structure-function correlations in this class of metalloproteins.Keywords
This publication has 22 references indexed in Scilit:
- Comparison of the solution conformations of human [Zn7]-metallothionein-2 and [Cd7]-metallothionein-2 using nuclear magnetic resonance spectroscopyJournal of Molecular Biology, 1992
- High-resolution solution structure of reduced French bean plastocyanin and comparison with the crystal structure of poplar plastocyaninJournal of Molecular Biology, 1991
- Comparison of the high-resolution structures of the α-amylase inhibitor tendamistat determined by nuclear magnetic resonance in solution and by X-ray diffraction in single crystalsJournal of Molecular Biology, 1989
- Solution of the phase problem in the X-ray diffraction method for proteins with the nuclear magnetic resonance solution structure as initial modelJournal of Molecular Biology, 1989
- Conformation of [Cd7]-metallothionein-2 from rat liver in aqueous solution determined by nuclear magnetic resonance spectroscopyJournal of Molecular Biology, 1988
- Three-dimensional structure of rabbit liver [Cd7]metallothionein-2a in aqueous solution determined by nuclear magnetic resonanceJournal of Molecular Biology, 1988
- METALLOTHIONEINAnnual Review of Biochemistry, 1986
- Nuclear magnetic resonance identification of “half-turn” and 310-helix secondary structure in rabbit liver metallothionein-2Journal of Molecular Biology, 1986
- Calculation of protein conformations by proton-proton distance constraintsJournal of Molecular Biology, 1985
- Solvent accessible surface area and excluded volume in proteinsJournal of Molecular Biology, 1984