2POH

Structure of Phage P22 Tail Needle gp26

2POH の概要

• エントリーDOI: 10.2210/pdb2poh/pdb
• 関連するPDBエントリー: 1LKT
• 分子名称: Head completion protein (2 entities in total)
• 機能のキーワード: trimeric coiled-coil, triple beta-helix, heptad, membrane-penetration, fiber, viral protein
• 由来する生物種: Salmonella phage P22-pbi
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 149143.28

構造登録者

Olia, A.S.,Cingolani, G. (登録日: 2007-04-26, 公開日: 2007-12-04, 最終更新日: 2024-10-30)

主引用文献

Olia, A.S.,Casjens, S.,Cingolani, G.
Structure of phage P22 cell envelope-penetrating needle.
Nat.Struct.Mol.Biol., 14:1221-1226, 2007

PubMed Abstract: Bacteriophage P22 infects Salmonella enterica by injecting its genetic material through the cell envelope. During infection, a specialized tail needle, gp26, is injected into the host, likely piercing a hole in the host cell envelope. The 2.1-Å crystal structure of gp26 reveals a 240-Å elongated protein fiber formed by two trimeric coiled-coil domains interrupted by a triple β-helix.The N terminus of gp26 plugs the portal protein channel, retaining the genetic material inside the virion. The C-terminal tip of the fiber exposes β-hairpins with hydrophobic tips similar to those seen in class II fusion peptides. The α-helical core connecting these two functionally polarized tips presents four trimerization octads with consensus sequence IXXLXXXV. The slender conformation of the gp26 fiber minimizes the surface exposed to solvent, which is consistent with the idea that gp26 traverses the cell envelope lipid bilayers.

PubMed: 18059287
DOI: 10.1038/nsmb1317

実験手法

X-RAY DIFFRACTION (2.1 Å)