Three-dimensional structure of human [113Cd7]metallothionein-2 in solution determined by nuclear magnetic resonance spectroscopy.
The three-dimensional structure of human [113Cd7]metallothionein-2 was determined by nuclear magnetic resonance spectroscopy in solution. Sequence-specific 1H resonance assignments were obtained using the sequential assignment method. The input for the structure calculations consisted of the metal-cysteine co-ordinative bonds identified with heteronuclear correlation spectroscopy, 1H-1H distance constraints from nuclear Overhauser enhancement spectroscopy, and spin-spin coupling constants 3JHN alpha and 3J alpha beta. The molecule consists of two domains, the beta-domain including amino acid residues 1 to 30 and three metal ions, and the alpha-domain including residues 31 to 61 and four metal ions. The nuclear magnetic resonance data present no evidence for a preferred relative orientation of the two domains. The polypeptide-to-metal co-ordinative bonds in human metallothionein-2 are identical to those in the previously determined solution structures of rat metallothionein-2 and rabbit metallothionein-2a, and the polypeptide conformations in the three proteins are also closely similar.
Messerle
B A
BA
Institut für Molekularbiologie und Biophysik, Hochschule-Hönggerberg, Zürich, Switzerland.
Schäffer
A
A
Vasák
M
M
Kägi
J H
JH
Wüthrich
K
K
D000595:Amino Acid Sequence; D000818:Animals; D002104:Cadmium; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008668:Metallothionein; D008969:Molecular Sequence Data; D015394:Molecular Structure; D011487:Protein Conformation; D051381:Rats; D012689:Sequence Homology, Nucleic Acid; D012996:Solutions; D013237:Stereoisomerism
D012996:Solutions; C004203:cadmium-binding protein; D002104:Cadmium; D008668:Metallothionein