1YXN

Pseudo-atomic model of a fiberless isometric variant of bacteriophage phi29

1YXN の概要

• エントリーDOI: 10.2210/pdb1yxn/pdb
• 関連するPDBエントリー: 1F00 1OHG
• EMDBエントリー: 1116 1120
• 分子名称: Major head protein (1 entity in total)
• 機能のキーワード: phi29, capsid, icosahedral virus capsid, hk97 fold, phage, bacterial immuno-globulin, big2, icosahedral virus, virus
• 由来する生物種: Bacillus phage phi29
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 91967.00

構造登録者

Morais, M.C.,Choi, K.H.,Koti, J.S.,Chipman, P.R.,Anderson, D.L.,Rossmann, M.G. (登録日: 2005-02-22, 公開日: 2005-04-26, 最終更新日: 2024-02-14)

主引用文献

Morais, M.C.,Choi, K.H.,Koti, J.S.,Chipman, P.R.,Anderson, D.L.,Rossmann, M.G.
Conservation of the Capsid Structure in Tailed dsDNA Bacteriophages: the Pseudoatomic Structure of phi29
Mol.Cell, 18:149-159, 2005

PubMed Abstract: Bacteriophage phi29 is one of the smallest and simplest known dsDNA phages, making it amenable to structural investigations. The three-dimensional structure of a fiberless, isometric variant has been determined to 7.9 A resolution by cryo-electron microscopy (cryo-EM), allowing the identification of alpha helices and beta sheets. Their arrangement indicates that the folds of the phi29 and bacteriophage HK97 capsid proteins are similar except for an additional immunoglobulin-like domain of the phi29 protein. An atomic model that incorporates these two domains fits well into the cryo-EM density of the T = 3, fiberless isometric phi29 particle, and cryo-EM structures of fibered isometric and fiberless prolate prohead phi29 particles at resolutions of 8.7 A and 12.7 A, respectively. Thus, phi29 joins the growing number of phages that utilize the HK97 capsid structure, suggesting that this protein fold may be as prevalent in capsids of dsDNA phages as the jelly roll fold is in eukaryotic viruses.

PubMed: 15837419
DOI: 10.1016/j.molcel.2005.03.013

実験手法

ELECTRON MICROSCOPY (7.9 Å)