Structural studies of the contractile tail sheath protein of bacteriophage T4. 1. Conformational change of the tail sheath upon contraction as probed by differential chemical modification

Biochemistry ◽  
1990 ◽  
Vol 29 (21) ◽  
pp. 5050-5056 ◽  
Author(s):  
Shigeki Takeda ◽  
Fumio Arisaka ◽  
Shinichi Ishii ◽  
Yoshimasa Kyogoku
Keyword(s):  
Chemical Modification ◽  
Conformational Change ◽  
Bacteriophage T4 ◽  
Structural Studies ◽  
Tail Sheath ◽  
Contractile Tail

scholarly journals Structural Analysis of Jumbo Coliphage phAPEC6

2020 ◽  
Vol 21 (9) ◽  
pp. 3119 ◽  
Author(s):  
Jeroen Wagemans ◽  
Jessica Tsonos ◽  
Dominique Holtappels ◽  
Kiandro Fortuna ◽  
Jean-Pierre Hernalsteens ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Capsid Protein ◽  
Tem Analysis ◽  
Host Interaction ◽  
Cryo Electron Microscopy ◽  
Transmission Electron ◽  
Tail Sheath ◽  
Associated Proteins ◽  
Contractile Tail ◽  
Phage Capsid

The phAPEC6 genome encodes 551 predicted gene products, with the vast majority (83%) of unknown function. Of these, 62 have been identified as virion-associated proteins by mass spectrometry (ESI-MS/MS), including the major capsid protein (Gp225; present in 1620 copies), which shows a HK97 capsid protein-based fold. Cryo-electron microscopy experiments showed that the 350-kbp DNA molecule of Escherichia coli virus phAPEC6 is packaged in at least 15 concentric layers in the phage capsid. A capsid inner body rod is also present, measuring about 91 nm by 18 nm and oriented along the portal axis. In the phAPEC6 contractile tail, 25 hexameric stacked rings can be distinguished, built of the identified tail sheath protein (Gp277). Cryo-EM reconstruction reveals the base of the unique hairy fibers observed during an initial transmission electron microscopy (TEM) analysis. These very unusual filaments are ordered at three annular positions along the contractile sheath, as well as around the capsid, and may be involved in host interaction.

Tail Components of T2 Bacteriophage. I. Properties of the Isolated Contractile Tail Sheath*

Biochemistry ◽  
1964 ◽  
Vol 3 (4) ◽  
pp. 511-517 ◽  
Author(s):  
Nilima Sarkar ◽  
Satyapriya Sarkar ◽  
L. M. Kozloff
Keyword(s):  
Tail Sheath ◽  
Contractile Tail

scholarly journals The tail sheath structure of bacteriophage T4: a molecular machine for infecting bacteria

2012 ◽  
Vol 31 (16) ◽  
pp. 3507-3507 ◽  
Author(s):  
Anastasia A Aksyuk ◽  
Petr G Leiman ◽  
Lidia P Kurochkina ◽  
Mikhail M Shneider ◽  
Victor A Kostyuchenko ◽  
...  
Keyword(s):  
Bacteriophage T4 ◽  
Molecular Machine ◽  
Tail Sheath ◽  
Sheath Structure

Polymerization of Bacteriophage T4 Tail Sheath Protein Mutants Truncated at the C-Termini

1999 ◽  
Vol 127 (3) ◽  
pp. 224-230 ◽  
Author(s):  
Boris F. Poglazov ◽  
Andrei V. Efimov ◽  
Sergio Marco ◽  
Jose Carrascosa ◽  
Tanya A. Kuznetsova ◽  
...  
Keyword(s):  
Bacteriophage T4 ◽  
Protein Mutants ◽  
Tail Sheath

scholarly journals A First Model of the Dynamics of the Bacteriophage T4 Injection Machinery

2016 ◽  
Vol 11 (4) ◽  
Author(s):  
Ameneh Maghsoodi ◽  
Anupam Chatterjee ◽  
Ioan Andricioaei ◽  
N. C. Perkins
Keyword(s):  
Bacteriophage T4 ◽  
Infection Process ◽  
Hydrodynamic Drag ◽  
Kirchhoff Rod ◽  
Rod Theory ◽  
Tail Assembly ◽  
Contractile Tail ◽  
Helical Protein ◽  
Important Building Block ◽  
Sheath Structure

Bacteriophage T4 is one of the most common and complex of the tailed viruses that infect host bacteria using an intriguing contractile tail assembly. Despite extensive progress in resolving the structure of T4, the dynamics of the injection machinery remains largely unknown. This paper contributes a first model of the injection machinery that is driven by elastic energy stored in a structure known as the sheath. The sheath is composed of helical strands of protein that suddenly collapse from an energetic, extended conformation prior to infection to a relaxed, contracted conformation during infection. We employ Kirchhoff rod theory to simulate the nonlinear dynamics of a single protein strand coupled to a model for the remainder of the virus, including the coupled translation and rotation of the head (capsid), neck, and tail tube. Doing so provides an important building block toward the future goal of modeling the entire sheath structure which is composed of six interacting helical protein strands. The resulting numerical model exposes fundamental features of the injection machinery including the time scale and energetics of the infection process, the nonlinear conformational change experienced by the sheath, and the contribution of hydrodynamic drag on the head (capsid).

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