2mrb | pdb_00002mrb

THREE-DIMENSIONAL STRUCTURE OF RABBIT LIVER CD-7 METALLOTHIONEIN-2A IN AQUEOUS SOLUTION DETERMINED BY NUCLEAR MAGNETIC RESONANCE

spinqualitylabelsall models 2mrb Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2mrb is a 1 chain structure with sequence from Oryctolagus cuniculus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Ligands: CD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MT2A_RABIT Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids. Publication Abstract from PubMed In previous work the metal-polypeptide co-ordinative bonds in the major protein species of a reconstituted [113Cd7]metallothionein-2 preparation from rabbit liver in aqueous solution were determined, the secondary polypeptide structure was found to contain several half-turns and 3(10)-helical segments, and a preliminary characterization of the overall polypeptide backbone fold in the beta-domain containing the three-metal cluster, and the alpha-domain containing the four-metal cluster, was obtained. Using a new, more extensive set of nuclear magnetic resonance data these earlier structures were improved by new structure calculations. The new experimental data consist of distance constraints from measurements of nuclear Overhauser effects, and dihedral angle constraints derived from both coupling constants and nuclear Overhauser effects. The structure calculations were performed with the program DISMAN. Since no information on the orientation of the two domains relative to each other could be obtained, the structure calculations were performed separately for the alpha-domain and the beta-domain. The average of the pairwise root-mean-square distances among the 20 structures with the least residual violations of input constraints was 2.9 A for the beta-domain and 1.4 A for the alpha-domain (1 A = 0.1 nm). The overall chirality of the polypeptide fold is right-handed for the beta-domain and left-handed for the alpha-domain. For each of the seven metal ions the local chirality of the co-ordination of the four cysteinyl Sy atoms is clearly defined. The improved structures of both domains show the previously noted differences relative to the recently published crystal structure of metallothionein-2a from rat liver. Three-dimensional structure of rabbit liver [Cd7]metallothionein-2a in aqueous solution determined by nuclear magnetic resonance.,Arseniev A, Schultze P, Worgotter E, Braun W, Wagner G, Vasak M, Kagi JH, Wuthrich K J Mol Biol. 1988 Jun 5;201(3):637-57. PMID:3418714 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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