2XVR
Phage T7 empty mature head shell
2XVR の概要
| エントリーDOI | 10.2210/pdb2xvr/pdb |
| EMDBエントリー | 1810 |
| 分子名称 | MAJOR CAPSID PROTEIN 10A (1 entity in total) |
| 機能のキーワード | virus, capsid maturation, morphogenetic intermediate |
| 由来する生物種 | ENTEROBACTERIA PHAGE T7 |
| タンパク質・核酸の鎖数 | 7 |
| 化学式量合計 | 256127.38 |
| 構造登録者 | Ionel, A.,Velazquez-Muriel, J.A.,Luque, D.,Cuervo, A.,Caston, J.R.,Valpuesta, J.M.,Martin-Benito, J.,Carrascosa, J.L. (登録日: 2010-10-28, 公開日: 2010-12-01, 最終更新日: 2024-05-08) |
| 主引用文献 | Ionel, A.,Velazquez-Muriel, J.A.,Luque, D.,Cuervo, A.,Caston, J.R.,Valpuesta, J.M.,Martin-Benito, J.,Carrascosa, J.L. Molecular Rearrangements Involved in the Capsid Shell Maturation of Bacteriophage T7. J.Biol.Chem., 286:234-, 2011 Cited by PubMed Abstract: Maturation of dsDNA bacteriophages involves assembling the virus prohead from a limited set of structural components followed by rearrangements required for the stability that is necessary for infecting a host under challenging environmental conditions. Here, we determine the mature capsid structure of T7 at 1 nm resolution by cryo-electron microscopy and compare it with the prohead to reveal the molecular basis of T7 shell maturation. The mature capsid presents an expanded and thinner shell, with a drastic rearrangement of the major protein monomers that increases in their interacting surfaces, in turn resulting in a new bonding lattice. The rearrangements include tilting, in-plane rotation, and radial expansion of the subunits, as well as a relative bending of the A- and P-domains of each subunit. The unique features of this shell transformation, which does not employ the accessory proteins, inserted domains, or molecular interactions observed in other phages, suggest a simple capsid assembling strategy that may have appeared early in the evolution of these viruses. PubMed: 20962334DOI: 10.1074/JBC.M110.187211 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (10.8 Å) |
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