1GW7

QUASI-ATOMIC RESOLUTION MODEL OF BACTERIOPHAGE PRD1 CAPSID, OBTAINED BY COMBINED CRYO-EM AND X-RAY CRYSTALLOGRAPHY.

1GW7 の概要

• エントリーDOI: 10.2210/pdb1gw7/pdb
• 関連するPDBエントリー: 1CJD 1GW8 1HB5 1HB7 1HQN 1HX6
• EMDBエントリー: 1011
• 分子名称: MAJOR CAPSID PROTEIN (1 entity in total)
• 機能のキーワード: virus/viral protein, tectiviridae, bacteriophage prd1, cryo- em, image reconstruction, icosahedral virus, virus-viral protein complex
• 由来する生物種: BACTERIOPHAGE PRD1
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 520154.63

構造登録者

San Martin, C.,Huiskonen, J.,Bamford, J.K.H.,Butcher, S.J.,Fuller, S.D.,Bamford, D.H.,Burnett, R.M. (登録日: 2002-03-08, 公開日: 2002-03-13, 最終更新日: 2024-05-08)

主引用文献

San Martin, C.,Huiskonen, J.,Bamford, J.K.H.,Butcher, S.J.,Fuller, S.D.,Bamford, D.H.,Burnett, R.M.
Minor Proteins, Mobile Arms, and Membrane-Capsid Interactions in Bacteriophage Prd1 Capsid Assembly
Nat.Struct.Biol., 9:756-, 2002

PubMed Abstract: Bacteriophage PRD1 shares many structural and functional similarities with adenovirus. A major difference is the PRD1 internal membrane, which acts in concert with vertex proteins to translocate the phage genome into the host. Multiresolution models of the PRD1 capsid, together with genetic analyses, provide fine details of the molecular interactions associated with particle stability and membrane dynamics. The N- and C-termini of the major coat protein (P3), which are required for capsid assembly, act as conformational switches bridging capsid to membrane and linking P3 trimers. Electrostatic P3-membrane interactions increase virion stability upon DNA packaging. Newly revealed proteins suggest how the metastable vertex works and how the capsid edges are stabilized.

PubMed: 12219080
DOI: 10.1038/NSB837

実験手法

ELECTRON MICROSCOPY (13.5 Å)