4mt2

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spinqualitylabelsall models 4mt2, resolution 2.0Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

COMPARISON OF THE NMR SOLUTION STRUCTURE AND THE X-RAY CRYSTAL STRUCTURE OF RAT METALLOTHIONEIN-2

Overview

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.

About this Structure

4MT2 is a Single protein structure of sequence from Rattus rattus with CD, ZN, NA and ACE as ligands. Full crystallographic information is available from OCA.

Reference

Comparison of the NMR solution structure and the x-ray crystal structure of rat metallothionein-2., Braun W, Vasak M, Robbins AH, Stout CD, Wagner G, Kagi JH, Wuthrich K, Proc Natl Acad Sci U S A. 1992 Nov 1;89(21):10124-8. PMID:1438200

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