EMD-20961
C5 reconstruction of bacteriophage T4 portal vertex
EMD-20961
Single-particle3.4 Å
Deposition: 15/11/2019
Map released: 22/04/2020
Last modified: 22/04/2020
Sample Organism:
Escherichia virus T4
Sample: Escherichia virus T4
Deposition Authors: Fang Q, Fokine A, Rossmann MG, Rao VB
Sample: Escherichia virus T4
Deposition Authors: Fang Q, Fokine A, Rossmann MG, Rao VB
Structural morphing in a symmetry-mismatched viral vertex.
Fang Q,
Tang WC,
Tao P ,
Mahalingam M,
Fokine A,
Rossmann MG,
Rao VB
(2020) Nat Commun , 11 , 1713 - 1713
(2020) Nat Commun , 11 , 1713 - 1713
Abstract:
Large biological structures are assembled from smaller, often symmetric, sub-structures. However, asymmetry among sub-structures is fundamentally important for biological function. An extreme form of asymmetry, a 12-fold-symmetric dodecameric portal complex inserted into a 5-fold-symmetric capsid vertex, is found in numerous icosahedral viruses, including tailed bacteriophages, herpesviruses, and archaeal viruses. This vertex is critical for driving capsid assembly, DNA packaging, tail attachment, and genome ejection. Here, we report the near-atomic in situ structure of the symmetry-mismatched portal vertex from bacteriophage T4. Remarkably, the local structure of portal morphs to compensate for symmetry-mismatch, forming similar interactions in different capsid environments while maintaining strict symmetry in the rest of the structure. This creates a unique and unusually dynamic symmetry-mismatched vertex that is central to building an infectious virion.
Large biological structures are assembled from smaller, often symmetric, sub-structures. However, asymmetry among sub-structures is fundamentally important for biological function. An extreme form of asymmetry, a 12-fold-symmetric dodecameric portal complex inserted into a 5-fold-symmetric capsid vertex, is found in numerous icosahedral viruses, including tailed bacteriophages, herpesviruses, and archaeal viruses. This vertex is critical for driving capsid assembly, DNA packaging, tail attachment, and genome ejection. Here, we report the near-atomic in situ structure of the symmetry-mismatched portal vertex from bacteriophage T4. Remarkably, the local structure of portal morphs to compensate for symmetry-mismatch, forming similar interactions in different capsid environments while maintaining strict symmetry in the rest of the structure. This creates a unique and unusually dynamic symmetry-mismatched vertex that is central to building an infectious virion.