7VI9

Cryo-EM structure of bacteriophage lambda procapsid at 5.03 Angstrom

Summary for 7VI9

• Entry DOI: 10.2210/pdb7vi9/pdb
• EMDB information: 32004
• Descriptor: Major capsid protein (1 entity in total)
• Functional Keywords: bacteriophage lambda; capsid; procapsid; capsid maturation; virus structure; cryo-em; auxiliary protein; conformational expansion; cementing protein; dna packaging, virus
• Biological source: Escherichia phage lambda (Bacteriophage lambda)
• Total number of polymer chains: 7
• Total formula weight: 267604.12

Authors

Wang, J.W. (deposition date: 2021-09-26, release date: 2021-12-15, Last modification date: 2024-06-19)

Primary citation

Wang, C.,Zeng, J.,Wang, J.
Structural basis of bacteriophage lambda capsid maturation.
Structure, 30:637-, 2022

PubMed Abstract: Bacteriophage lambda is an excellent model system for studying capsid assembly of double-stranded DNA (dsDNA) bacteriophages, some dsDNA archaeal viruses, and herpesviruses. HK97 fold coat proteins initially assemble into a precursor capsid (procapsid) and subsequent genome packaging triggers morphological expansion of the shell. An auxiliary protein is required to stabilize the expanded capsid structure. To investigate the capsid maturation mechanism, we determined the cryo-electron microscopy structures of the bacteriophage lambda procapsid and mature capsid at 3.88 Å and 3.76 Å resolution, respectively. Besides primarily rigid body movements of common features of the major capsid protein gpE, large-scale structural rearrangements of other domains occur simultaneously. Assembly of intercapsomers within the procapsid is facilitated by layer-stacking effects at 3-fold vertices. Upon conformational expansion of the capsid shell, the missing top layer is fulfilled by cementing the gpD protein against the internal pressure of DNA packaging. Our structures illuminate the assembly mechanisms of dsDNA viruses.

PubMed: 35026161
DOI: 10.1016/j.str.2021.12.009

Experimental method

ELECTRON MICROSCOPY (5.03 Å)