1H5W

2.1A Bacteriophage Phi-29 Connector

1H5W の概要

• エントリーDOI: 10.2210/pdb1h5w/pdb
• 関連するPDBエントリー: 1FOU 1IJG
• 分子名称: UPPER COLLAR PROTEIN, (4S)-2-METHYL-2,4-PENTANEDIOL (3 entities in total)
• 機能のキーワード: virus, connector, portal, sh3-like, helix bundle
• 由来する生物種: BACTERIOPHAGE PHI-29
• 細胞内の位置: Virion : P04332
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 108224.57

構造登録者

Guasch, A.,Pous, J.,Ibarra, B.,Gomis-Ruth, F.X.,Valpuesta, J.M.,Sousa, N.,Carrascosa, J.L.,Coll, M. (登録日: 2001-05-28, 公開日: 2002-02-13, 最終更新日: 2023-12-13)

主引用文献

Guasch, A.,Pous, J.,Ibarra, B.,Gomis-Ruth, F.X.,Valpuesta, J.M.,Sousa, N.,Carrascosa, J.L.,Coll, M.
Detailed Architecture of a DNA Translocating Machine: The High-Resolution Structure of the Bacteriophage Phi29 Connector Particle.
J.Mol.Biol., 315:663-, 2002

PubMed Abstract: The three-dimensional crystal structure of the bacteriophage phi29 connector has been solved and refined to 2.1A resolution. This 422 kDa oligomeric protein connects the head of the phage to its tail and translocates the DNA into the prohead during packaging. Each monomer has an elongated shape and is composed of a central, mainly alpha-helical domain that includes a three-helix bundle, a distal alpha/beta domain and a proximal six-stranded SH3-like domain. The protomers assemble into a 12-mer, propeller-like, super-structure with a 35 A wide central channel. The surface of the channel is mainly electronegative, but it includes two lysine rings 20 A apart. On the external surface of the particle a hydrophobic belt extends to the concave area below the SH3-like domain, which forms a crown that retains the particle in the head. The lipophilic belt contacts the non-matching symmetry vertex of the capsid and forms a bearing for the connector rotation. The structure suggests a translocation mechanism in which the longitudinal displacement of the DNA along its axis is coupled to connector spinning.

PubMed: 11812138
DOI: 10.1006/JMBI.2001.5278

実験手法

X-RAY DIFFRACTION (2.1 Å)