6UZC

Portal vertex structure of bacteriophage T4

This is a non-PDB format compatible entry.

Summary for 6UZC

• Entry DOI: 10.2210/pdb6uzc/pdb
• EMDB information: 20956
• Descriptor: Major capsid protein, Portal protein (2 entities in total)
• Functional Keywords: portal protein assembly, gp20, gp23, portal vertex, virus
• Biological source: Enterobacteria phage T4; More
• Total number of polymer chains: 42
• Total formula weight: 2415632.24

Authors

Fang, Q.,Fokine, A.,Rao, V.B. (deposition date: 2019-11-14, release date: 2020-04-29, Last modification date: 2024-03-06)

Primary citation

Fang, Q.,Tang, W.C.,Tao, P.,Mahalingam, M.,Fokine, A.,Rossmann, M.G.,Rao, V.B.
Structural morphing in a symmetry-mismatched viral vertex.
Nat Commun, 11:1713-1713, 2020

PubMed 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.

PubMed: 32249784
DOI: 10.1038/s41467-020-15575-4

Experimental method

ELECTRON MICROSCOPY (4.5 Å)