5IW9

Structure of bacteriophage T4 gp25, sheath polymerization initiator

「4HRZ」から置き換えられました

5IW9 の概要

• エントリーDOI: 10.2210/pdb5iw9/pdb
• 分子名称: Baseplate wedge protein gp25 (2 entities in total)
• 機能のキーワード: contractile sheath, baseplate, wedge, sheath polymerization, viral protein
• 由来する生物種: Enterobacteria phage T4
• 細胞内の位置: Virion : P09425
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 30241.18

構造登録者

Leiman, P.G.,Browning, C.,Shneider, M.M. (登録日: 2016-03-22, 公開日: 2016-05-11, 最終更新日: 2024-11-20)

主引用文献

Taylor, N.M.,Prokhorov, N.S.,Guerrero-Ferreira, R.C.,Shneider, M.M.,Browning, C.,Goldie, K.N.,Stahlberg, H.,Leiman, P.G.
Structure of the T4 baseplate and its function in triggering sheath contraction.
Nature, 533:346-352, 2016

PubMed Abstract: Several systems, including contractile tail bacteriophages, the type VI secretion system and R-type pyocins, use a multiprotein tubular apparatus to attach to and penetrate host cell membranes. This macromolecular machine resembles a stretched, coiled spring (or sheath) wound around a rigid tube with a spike-shaped protein at its tip. A baseplate structure, which is arguably the most complex part of this assembly, relays the contraction signal to the sheath. Here we present the atomic structure of the approximately 6-megadalton bacteriophage T4 baseplate in its pre- and post-host attachment states and explain the events that lead to sheath contraction in atomic detail. We establish the identity and function of a minimal set of components that is conserved in all contractile injection systems and show that the triggering mechanism is universally conserved.

PubMed: 27193680
DOI: 10.1038/nature17971

実験手法

X-RAY DIFFRACTION (2.47 Å)