8JAN の概要
| エントリーDOI | 10.2210/pdb8jan/pdb |
| EMDBエントリー | 36130 |
| 分子名称 | BplB, Gp22, Gp24 (3 entities in total) |
| 機能のキーワード | complex, phage, virus, viral protein |
| 由来する生物種 | Escherichia phage P1 詳細 |
| タンパク質・核酸の鎖数 | 30 |
| 化学式量合計 | 1083422.52 |
| 構造登録者 | |
| 主引用文献 | Yang, F.,Wang, L.,Zhou, J.,Xiao, H.,Liu, H. In Situ Structures of the Ultra-Long Extended and Contracted Tail of Myoviridae Phage P1. Viruses, 15:-, 2023 Cited by PubMed Abstract: The phage tail is a common component of contractile injection systems (CISs), essential for exerting contractile function and facilitating membrane penetration of the inner tail tube. The near-atomic resolution structures of the tail have been extensively studied, but the dynamic conformational changes before and after contraction and the associated molecular mechanism are still unclear. Here, we present the extended and contracted intact tail-structures of phage P1 by cryo-EM. The ultra-long tail of P1, 2450 Å in length, consists of a neck, a tail terminator, 53 repeated tail sheath rings, 53 repeated tube rings, and a baseplate. The sheath of the contracted tail shrinks by approximately 55%, resulting in the separation of the inner rigid tail tube from the sheath. The extended and contracted tails were further resolved by local reconstruction at 3.3 Å and 3.9 Å resolutions, respectively, allowing us to build the atomic models of the tail terminator protein gp24, the tube protein BplB, and the sheath protein gp22 for the extended tail, and of the sheath protein gp22 for the contracted tail. Our atomic models reveal the complex interaction network in the ultra-long tail and the novel conformational changes of the tail sheath between extended and contracted states. Our structures provide insights into the contraction and stabilization mechanisms of the tail. PubMed: 37376567DOI: 10.3390/v15061267 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.3 Å) |
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