1AA0
FIBRITIN DELETION MUTANT E (BACTERIOPHAGE T4)
1AA0 の概要
| エントリーDOI | 10.2210/pdb1aa0/pdb |
| 分子名称 | FIBRITIN, CHLORIDE ION, ZINC ION, ... (4 entities in total) |
| 機能のキーワード | bacteriophage t4, fibritin, structural protein, bacteriophage assembly, attachment protein |
| 由来する生物種 | Enterobacteria phage T4 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 11959.84 |
| 構造登録者 | Tao, Y.,Strelkov, S.V.,Mesyanzhinov, V.V.,Rossmann, M.G. (登録日: 1997-01-18, 公開日: 1997-07-23, 最終更新日: 2024-02-07) |
| 主引用文献 | Tao, Y.,Strelkov, S.V.,Mesyanzhinov, V.V.,Rossmann, M.G. Structure of bacteriophage T4 fibritin: a segmented coiled coil and the role of the C-terminal domain. Structure, 5:789-798, 1997 Cited by PubMed Abstract: Oligomeric coiled-coil motifs are found in numerous protein structures; among them is fibritin, a structural protein of bacteriophage T4, which belongs to a class of chaperones that catalyze a specific phage-assembly process. Fibritin promotes the assembly of the long tail fibers and their subsequent attachment to the tail baseplate; it is also a sensing device that controls the retraction of the long tail fibers in adverse environments and, thus, prevents infection. The structure of fibritin had been predicted from sequence and biochemical analyses to be mainly a triple-helical coiled coil. The determination of its structure at atomic resolution was expected to give insights into the assembly process and biological function of fibritin, and the properties of modified coiled-coil structures in general. PubMed: 9261070DOI: 10.1016/S0969-2126(97)00233-5 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.2 Å) |
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