7SQU

Goslar chimallin C4 tetramer localized reconstruction

Summary for 7SQU

• Entry DOI: 10.2210/pdb7squ/pdb
• EMDB information: 25183 25220 25221 25222 25223 25229 25262 25358 25359 25360 25390 25391 25392 25393 25394 25395 25396
• Descriptor: Chimallin (1 entity in total)
• Functional Keywords: phage, viral protein, structural protein
• Biological source: Escherichia phage vB_EcoM_Goslar
• Total number of polymer chains: 12
• Total formula weight: 838673.34

Authors

Laughlin, T.G.,Deep, A.,Prichard, A.M.,Seitz, C.,Gu, Y.,Enustun, E.,Suslov, S.,Khanna, K.,Birkholz, E.A.,Amaro, R.E.,Pogliano, J.,Corbett, K.D.,Villa, E. (deposition date: 2021-11-06, release date: 2022-07-27, Last modification date: 2024-06-05)

Primary citation

Laughlin, T.G.,Deep, A.,Prichard, A.M.,Seitz, C.,Gu, Y.,Enustun, E.,Suslov, S.,Khanna, K.,Birkholz, E.A.,Armbruster, E.,McCammon, J.A.,Amaro, R.E.,Pogliano, J.,Corbett, K.D.,Villa, E.
Architecture and self-assembly of the jumbo bacteriophage nuclear shell.
Nature, 608:429-435, 2022

PubMed Abstract: Bacteria encode myriad defences that target the genomes of infecting bacteriophage, including restriction-modification and CRISPR-Cas systems. In response, one family of large bacteriophages uses a nucleus-like compartment to protect its replicating genomes by excluding host defence factors. However, the principal composition and structure of this compartment remain unknown. Here we find that the bacteriophage nuclear shell assembles primarily from one protein, which we name chimallin (ChmA). Combining cryo-electron tomography of nuclear shells in bacteriophage-infected cells and cryo-electron microscopy of a minimal chimallin compartment in vitro, we show that chimallin self-assembles as a flexible sheet into closed micrometre-scale compartments. The architecture and assembly dynamics of the chimallin shell suggest mechanisms for its nucleation and growth, and its role as a scaffold for phage-encoded factors mediating macromolecular transport, cytoskeletal interactions, and viral maturation.

PubMed: 35922510
DOI: 10.1038/s41586-022-05013-4

Experimental method

ELECTRON MICROSCOPY (2.6 Å)