7VII
cryoEM structure of bacteriophage lambda capsid at 5.6 Angstrom
Summary for 7VII
| Entry DOI | 10.2210/pdb7vii/pdb |
| EMDB information | 32004 32005 32010 |
| Descriptor | Major capsid protein, Capsid decoration protein (2 entities 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) More |
| Total number of polymer chains | 14 |
| Total formula weight | 348684.23 |
| Authors | Wang, J.W. (deposition date: 2021-09-27, 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 Cited by 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: 35026161DOI: 10.1016/j.str.2021.12.009 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (5.6 Å) |
Structure validation
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