6UZC の概要
エントリーDOI | 10.2210/pdb6uzc/pdb |
EMDBエントリー | 20956 |
分子名称 | Major capsid protein, Portal protein (2 entities in total) |
機能のキーワード | portal protein assembly, gp20, gp23, portal vertex, virus |
由来する生物種 | Enterobacteria phage T4 詳細 |
タンパク質・核酸の鎖数 | 42 |
化学式量合計 | 2415632.24 |
構造登録者 | |
主引用文献 | Fang, Q.,Tang, W.C.,Tao, P.,Mahalingam, M.,Fokine, A.,Rossmann, M.G.,Rao, V.B. Structural morphing in a symmetry-mismatched viral vertex. Nat Commun, 11:1713-1713, 2020 Cited by PubMed Abstract: Large biological structures are assembled from smaller, often symmetric, sub-structures. However, asymmetry among sub-structures is fundamentally important for biological function. An extreme form of asymmetry, a 12-fold-symmetric dodecameric portal complex inserted into a 5-fold-symmetric capsid vertex, is found in numerous icosahedral viruses, including tailed bacteriophages, herpesviruses, and archaeal viruses. This vertex is critical for driving capsid assembly, DNA packaging, tail attachment, and genome ejection. Here, we report the near-atomic in situ structure of the symmetry-mismatched portal vertex from bacteriophage T4. Remarkably, the local structure of portal morphs to compensate for symmetry-mismatch, forming similar interactions in different capsid environments while maintaining strict symmetry in the rest of the structure. This creates a unique and unusually dynamic symmetry-mismatched vertex that is central to building an infectious virion. PubMed: 32249784DOI: 10.1038/s41467-020-15575-4 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (4.5 Å) |
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