4BML

C-alpha backbone trace of major capsid protein gp39 found in marine virus Syn5.

4BML の概要

• エントリーDOI: 10.2210/pdb4bml/pdb
• EMDBエントリー: 5954
• 分子名称: MAJOR CAPSID PROTEIN (1 entity in total)
• 機能のキーワード: virus, marine virus, outer capsid protein, maturation
• 由来する生物種: SYNECHOCOCCUS PHAGE SYN5 (HORNED VIRUS SYN5)
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 245741.86

構造登録者

Gipson, P.,Baker, M.L.,Raytcheva, D.,Haase-Pettingell, C.,Piret, J.,King, J.,Chiu, W. (登録日: 2013-05-09, 公開日: 2014-05-21, 最終更新日: 2024-05-08)

主引用文献

Gipson, P.,Baker, M.L.,Raytcheva, D.,Haase-Pettingell, C.,Piret, J.,King, J.A.,Chiu, W.
Protruding Knob-Like Proteins Violate Local Symmetries in an Icosahedral Marine Virus.
Nat.Commun., 5:4278-, 2014

PubMed Abstract: Marine viruses play crucial roles in shaping the dynamics of oceanic microbial communities and in the carbon cycle on Earth. Here we report a 4.7-Å structure of a cyanobacterial virus, Syn5, by electron cryo-microscopy and modelling. A Cα backbone trace of the major capsid protein (gp39) reveals a classic phage protein fold. In addition, two knob-like proteins protruding from the capsid surface are also observed. Using bioinformatics and structure analysis tools, these proteins are identified to correspond to gp55 and gp58 (each with two copies per asymmetric unit). The non 1:1 stoichiometric distribution of gp55/58 to gp39 breaks all expected local symmetries and leads to non-quasi-equivalence of the capsid subunits, suggesting a role in capsid stabilization. Such a structural arrangement has not yet been observed in any known virus structures.

PubMed: 24985522
DOI: 10.1038/NCOMMS5278

実験手法

ELECTRON MICROSCOPY (4.7 Å)