1MOG
Crystal structure of H. salinarum dodecin
1MOG の概要
エントリーDOI | 10.2210/pdb1mog/pdb |
分子名称 | Dodecin, MAGNESIUM ION, SODIUM ION, ... (6 entities in total) |
機能のキーワード | binding site for dimerized riboflavin, 23-symmetric dodecamer, unknown function |
由来する生物種 | Halobacterium salinarum |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 7829.73 |
構造登録者 | |
主引用文献 | Bieger, B.,Essen, L.-O.,Oesterhelt, D. Crystal Structure of Halophilic Dodecin: A Novel, Dodecameric Flavin Binding Protein from Halobacterium salinarum Structure, 11:375-385, 2003 Cited by PubMed Abstract: A novel, 68 amino acid long flavoprotein called dodecin has been discovered in the proteome of Halobacterium salinarum by inverse structural genomics. The 1.7 A crystal structure of this protein shows a dodecameric, hollow sphere-like arrangement of the protein subunits. Unlike other known flavoproteins, which bind only monomeric flavin cofactors, the structure of the dodecin oligomer comprises six riboflavin dimers. The dimerization of these riboflavins along the re-faces is mediated by aromatic, antiparallel pi staggering of their isoalloxazine moieties. A unique aromatic tetrade is formed by further sandwiching of the riboflavin dimers between the indole groups of two symmetry-related Trp36s. So far, the dodecins represent the smallest known flavoproteins. Based on the structure and the wide spread occurrences in pathogenic and soil eubacteria, a function in flavin storage or protection against radical or oxygenic stress is suggested for the dodecins. PubMed: 12679016DOI: 10.1016/S0969-2126(03)00048-0 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.7 Å) |
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