3GFD
Crystal structure of Mus musculus iodotyrosine deiodinase (IYD) bound to FMN and mono-iodotyrosine (MIT)
3GFD の概要
| エントリーDOI | 10.2210/pdb3gfd/pdb |
| 関連するPDBエントリー | 3GB5 3GH8 |
| 分子名称 | Iodotyrosine dehalogenase 1, FLAVIN MONONUCLEOTIDE, 3-IODO-TYROSINE, ... (5 entities in total) |
| 機能のキーワード | iyd, iodide salvage, flavoprotein, mono-iodotyrosine, mit, fmn, membrane, nadp, oxidoreductase, transmembrane |
| 由来する生物種 | Mus musculus (mouse) |
| 細胞内の位置 | Membrane; Single-pass membrane protein (By similarity): Q9DCX8 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 61777.94 |
| 構造登録者 | Thomas, S.R.,McTamney, P.M.,Adler, J.M.,LaRonde-LeBlanc, N.,Rokita, S.E. (登録日: 2009-02-26, 公開日: 2009-05-12, 最終更新日: 2023-09-06) |
| 主引用文献 | Thomas, S.R.,McTamney, P.M.,Adler, J.M.,Laronde-Leblanc, N.,Rokita, S.E. Crystal structure of iodotyrosine deiodinase, a novel flavoprotein responsible for iodide salvage in thyroid glands. J.Biol.Chem., 284:19659-19667, 2009 Cited by PubMed Abstract: The flavoprotein iodotyrosine deiodinase (IYD) salvages iodide from mono- and diiodotyrosine formed during the biosynthesis of the thyroid hormone thyroxine. Expression of a soluble domain of this membrane-bound enzyme provided sufficient material for crystallization and characterization by x-ray diffraction. The structures of IYD and two co-crystals containing substrates, mono- and diiodotyrosine, alternatively, were solved at resolutions of 2.0, 2.45, and 2.6 A, respectively. The structure of IYD is homologous to others in the NADH oxidase/flavin reductase superfamily, but the position of the active site lid in IYD defines a new subfamily within this group that includes BluB, an enzyme associated with vitamin B(12) biosynthesis. IYD and BluB also share key interactions involving their bound flavin mononucleotide that suggest a unique catalytic behavior within the superfamily. Substrate coordination to IYD induces formation of an additional helix and coil that act as an active site lid to shield the resulting substrate.flavin complex from solvent. This complex is stabilized by aromatic stacking and extensive hydrogen bonding between the substrate and flavin. The carbon-iodine bond of the substrate is positioned directly over the C-4a/N-5 region of the flavin to promote electron transfer. These structures now also provide a molecular basis for understanding thyroid disease based on mutations of IYD. PubMed: 19436071DOI: 10.1074/jbc.M109.013458 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.45 Å) |
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