6WKK
Phage G gp27 major capsid proteins and gp26 decoration proteins
6WKK の概要
エントリーDOI | 10.2210/pdb6wkk/pdb |
EMDBエントリー | 21695 21702 |
分子名称 | Gp27 major capsid protein, Gp26 capsid decoration protein (2 entities in total) |
機能のキーワード | phage g, major capsid protein, decoration protein, capsid, icosahedral, gp26, gp27, virus |
由来する生物種 | Bacillus virus G 詳細 |
タンパク質・核酸の鎖数 | 24 |
化学式量合計 | 469633.42 |
構造登録者 | |
主引用文献 | Gonzalez, B.,Monroe, L.,Li, K.,Yan, R.,Wright, E.,Walter, T.,Kihara, D.,Weintraub, S.T.,Thomas, J.A.,Serwer, P.,Jiang, W. Phage G Structure at 6.1 angstrom Resolution, Condensed DNA, and Host Identity Revision to a Lysinibacillus. J.Mol.Biol., 432:4139-4153, 2020 Cited by PubMed Abstract: Phage G has the largest capsid and genome of any known propagated phage. Many aspects of its structure, assembly, and replication have not been elucidated. Herein, we present the dsDNA-packed and empty phage G capsid at 6.1 and 9 Å resolution, respectively, using cryo-EM for structure determination and mass spectrometry for protein identification. The major capsid protein, gp27, is identified and found to share the HK97-fold universally conserved in all previously solved dsDNA phages. Trimers of the decoration protein, gp26, sit on the 3-fold axes and are thought to enhance the interactions of the hexameric capsomeres of gp27, for other phages encoding decoration proteins. Phage G's decoration protein is longer than what has been reported in other phages, and we suspect the extra interaction surface area helps stabilize the capsid. We identified several additional capsid proteins, including a candidate for the prohead protease responsible for processing gp27. Furthermore, cryo-EM reveals a range of partially full, condensed DNA densities that appear to have no contact with capsid shell. Three analyses confirm that the phage G host is a Lysinibacillus, and not Bacillus megaterium: identity of host proteins in our mass spectrometry analyses, genome sequence of the phage G host, and host range of phage G. PubMed: 32454153DOI: 10.1016/j.jmb.2020.05.016 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (6.1 Å) |
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