Structural morphing in a symmetry-mismatched viral vertex

Qianglin Fang, Wei-Chun Tang, Pan Tao, Marthandan Mahalingam, Andrei Fokine, Michael G. Rossmann and Venigalla B. Rao ()
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Qianglin Fang: Purdue University
Wei-Chun Tang: The Catholic University of America
Pan Tao: The Catholic University of America
Marthandan Mahalingam: The Catholic University of America
Andrei Fokine: Purdue University
Michael G. Rossmann: Purdue University
Venigalla B. Rao: The Catholic University of America

Nature Communications, 2020, vol. 11, issue 1, 1-11

Abstract: 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.

Date: 2020
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DOI: 10.1038/s41467-020-15575-4

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