Comparison of the NMR Solution Structure and the X-Ray Crystal Structure of Rat Metallothionein-2

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 89; no. 21; pp. 10124 - 10128
• Main Authors: Braun, W., Vasak, M., Robbins, A. H., Stout, C. D., Wagner, G., Kagi, J. H. R., Wuthrich, K.
• Format: Journal Article
• Language: English
• Published: Washington, DC National Academy of Sciences of the United States of America 01.11.1992; National Acad Sciences; National Academy of Sciences
• Subjects: Amino Acid Sequence; Amino acids; Analytical, structural and metabolic biochemistry; Animals; Architecture; Arithmetic mean; Atoms; Binding and carrier proteins; Binding Sites; Biological and medical sciences; Cadmium - analysis; Cellular biology; Crystal structure; Crystals; Cysteine; Fundamental and applied biological sciences. Psychology; Ions; Magnetic Resonance Spectroscopy - methods; Medical research; Metal ions; Metallothionein - genetics; metallothionein 2; Models, Molecular; Molecular structure; Molecules; N.M.R; Protein Conformation; Proteins; Rats; Rodents; Sulfur; X-Ray Diffraction - methods; Zinc - analysis; Binding protein; Vertebrata; Mammalia; Rat; Molecular structure; Rodentia; NMR spectrometry; X ray diffraction; Comparative study; Metallothionein
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.89.21.10124

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., Worgotter, E., Braun, W., Wagner, G., Vasak, M., Kagi, J. H. R. \& Wuthrich, 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.