Comparison of the NMR solution structure and the x-ray crystal structure of rat metallothionein-2.
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.
Braun
W
W
Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule, Zürich, Switzerland.
Vasák
M
M
Robbins
A H
AH
Stout
C D
CD
Wagner
G
G
Kägi
J H
JH
Wüthrich
K
K
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002104:Cadmium / Q000032:analysis; D003545:Cysteine; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008668:Metallothionein / Q000235:genetics*; D008958:Models, Molecular; D011487:Protein Conformation; D051381:Rats; D014961:X-Ray Diffraction / Q000379:methods; D015032:Zinc / Q000032:analysis
D002104:Cadmium; D008668:Metallothionein; D015032:Zinc; D003545:Cysteine