1dft
SOLUTION STRUCTURE OF THE BETA-DOMAIN OF MOUSE METALLOTHIONEIN-1
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OverviewOverview
Sequential 1H-NMR assignments of mouse [Cd7]-metallothionein-1 (MT1) have, been carried out by standard homonuclear NMR methods and the use of an, accordion-heteronuclear multiple quantum correlation (HMQC) experiment for, establishing the metal, 113Cd2+, to cysteine connectivities. The, three-dimensional structure was then calculated using the distance, constraints from two-dimensional nuclear Overhauser effect (NOE), spectroscopy spectra and the Cys-Cd connectivities as input for a distance, geometry-dynamical simulated annealing protocol in X-PLOR 3.851. Similar, to the mammalian MT2 isoforms, the homologous primary structure of MT1, suggested two separate domains, each containing one metal cluster. Because, there were no interdomain constraints, the structure calculation for the, N-terminal beta- and the C-terminal alpha-domain were carried out, separately. The structures are based on 409 NMR constraints, consisting of, 381 NOEs and 28 cysteine-metal connectivities. The only elements of, regular secondary structure found were two short stretches of 3(10), helices along with some half-turns in the alpha-domain. Structural, comparison with rat liver MT2 showed high similarity, with the beta-domain, structure in mouse MT1 showing evidence of increased flexibility compared, to the same domain in MT2. The latter was reflected by the presence of, fewer interresidue NOEs, no slowly exchanging backbone amide protons, and, enhanced cadmium-cadmium exchange rates found in the beta-domain of MT1.
About this StructureAbout this Structure
1DFT is a Single protein structure of sequence from Mus musculus with CD as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Three-dimensional solution structure of mouse [Cd7]-metallothionein-1 by homonuclear and heteronuclear NMR spectroscopy., Zangger K, Oz G, Otvos JD, Armitage IM, Protein Sci. 1999 Dec;8(12):2630-8. PMID:10631978
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