3to0

Crystal structure of Mus musculus iodotyrosine deiodinase (IYD) C217A, C239A bound to FMN

spinqualitylabelsall models 3to0, resolution 2.66Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3to0 is a 2 chain structure with sequence from Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT, FMN, PO4 Related: 3gb5, 3gfd, 3gh8, 3tnz Gene: IYD-1 (LK3 transgenic mice) Activity: Iodotyrosine deiodinase, with EC number 1.22.1.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [IYD1_MOUSE] Catalyzes the oxidative NADPH-dependent deiodination of monoiodotyrosine (L-MIT) or diiodotyrosine (L-DIT). Acts during the hydrolysis of thyroglobulin to liberate iodide, which can then reenter the hormone-producing pathways. Acts more efficiently on monoiodotyrosine than on diiodotyrosine (By similarity). Publication Abstract from PubMed Reductive deiodination is critical for thyroid function and represents an unusual exception to the more common oxidative and hydrolytic mechanisms of dehalogenation in mammals. Studies on the reductive processes have been limited by a lack of convenient methods for heterologous expression of the appropriate proteins in large scale. The enzyme responsible for iodide salvage in the thyroid, iodotyrosine deodinase, is now readily generated after engineering its gene from Mus musculus. High expression of a truncated derivative lacking the membrane domain at its N-terminal was observed in Sf9 cells whereas expression in Pichia pastoris remained low despite codon optimization. Ultimately, the desired expression in Escherichia coli was achieved after replacing the two conserved Cys residues of the deiodinase with Ala and fusing the resulting protein to thioredoxin. This final construct provided abundant enzyme for crystallography and mutagenesis. Utility of the E. coli system was demonstrated by examining a set of active site residues critical for binding to the zwitterionic portion of substrate. Expression of a soluble form of iodotyrosine deiodinase for active site characterization by engineering the native membrane protein from mus musculus.,Buss JM, McTamney PM, Rokita TE Protein Sci. 2012 Jan 11. doi: 10.1002/pro.2020. PMID:22238141 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Dehalogenase 3D structures

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