3ONS
Crystal structure of Human Ubiquitin in a new crystal form
3ONS の概要
エントリーDOI | 10.2210/pdb3ons/pdb |
分子名称 | Ubiquitin (2 entities in total) |
機能のキーワード | ubiquitin fold, signaling protein |
由来する生物種 | Homo sapiens (human) |
細胞内の位置 | Ubiquitin: Cytoplasm (By similarity): P0CG47 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 8192.38 |
構造登録者 | Amodeo, G.A.,Huang, K.Y.,Mcdermott, A.E.,Tong, L. (登録日: 2010-08-30, 公開日: 2011-02-23, 最終更新日: 2024-02-21) |
主引用文献 | Huang, K.Y.,Amodeo, G.A.,Tong, L.,McDermott, A. The structure of human ubiquitin in 2-methyl-2,4-pentanediol: a new conformational switch. Protein Sci., 20:630-639, 2011 Cited by PubMed Abstract: A new crystal structure of human ubiquitin is reported at 1.8 Å resolution. Compared with the other known crystal structure or the solution NMR structure of monomeric human ubiquitin, this new structure is similar in its overall fold but differs with respect to the conformation of the backbone in a surface-exposed region. The conformation reported here resembles conformations previously seen in complex with deubiquinating enzymes, wherein the Asp52/Gly53 main chain and Glu24 side chain move. This movement exposes the backbone carbonyl of Asp52 to the exterior of the molecule, making it possible to engage in hydrogen-bond contacts with neighboring molecules, rather than in an internal hydrogen bond with the backbone of Glu24. This particular crystal form of ubiquitin has been used in a large number of solid state NMR studies. The structure described here elucidates the origin of many of the chemical shift differences comparing solution and solid state studies. PubMed: 21432937DOI: 10.1002/pro.584 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.8 Å) |
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