Summary for 8XOT
| Entry DOI | 10.2210/pdb8xot/pdb |
| EMDB information | 38540 |
| Descriptor | Portal protein B (1 entity in total) |
| Functional Keywords | caudovirales, siphoviridae, portal vertex, portal, capsid, connector/neck, tail, delivery device, b-dna, viral protein |
| Biological source | Escherichia phage Lambda |
| Total number of polymer chains | 12 |
| Total formula weight | 714355.31 |
| Authors | Wang, J.W.,Gu, Z.W. (deposition date: 2024-01-02, release date: 2024-04-10, Last modification date: 2024-10-16) |
| Primary citation | Gu, Z.,Wu, K.,Wang, J. Structural morphing in the viral portal vertex of bacteriophage lambda. J.Virol., 98:e0006824-e0006824, 2024 Cited by PubMed Abstract: The portal protein of tailed bacteriophage plays essential roles in various aspects of capsid assembly, motor assembly, genome packaging, connector formation, and infection processes. After DNA packaging is complete, additional proteins are assembled onto the portal to form the connector complex, which is crucial as it bridges the mature head and tail. In this study, we report high-resolution cryo-electron microscopy (cryo-EM) structures of the portal vertex from bacteriophage lambda in both its prohead and mature virion states. Comparison of these structures shows that during head maturation, in addition to capsid expansion, the portal protein undergoes conformational changes to establish interactions with the connector proteins. Additionally, the independently assembled tail undergoes morphological alterations at its proximal end, facilitating its connection to the head-tail joining protein and resulting in the formation of a stable portal-connector-tail complex. The B-DNA molecule spirally glides through the tube, interacting with the nozzle blade region of the middle-ring connector protein. These insights elucidate a mechanism for portal maturation and DNA translocation within the phage lambda system. PubMed: 38661364DOI: 10.1128/jvi.00068-24 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.51 Å) |
Structure validation
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