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8XQB

Mature virion portal vertex of bacteriophage lambda

This is a non-PDB format compatible entry.
Summary for 8XQB
Entry DOI10.2210/pdb8xqb/pdb
EMDB information38540 38541 38542 38556 38572
DescriptorHead-tail connector protein FII, Head completion protein, Tail tube terminator protein, ... (6 entities in total)
Functional Keywordscaudovirales, siphoviridae, portal, capsid, connector/neck, tail, delivery device, b-dna, phage lambda, viral protein
Biological sourceEscherichia phage Lambda
More
Total number of polymer chains71
Total formula weight1775564.12
Authors
Wang, J.W.,Gu, Z.W. (deposition date: 2024-01-05, release date: 2024-04-10, Last modification date: 2024-10-30)
Primary citationGu, 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: 38661364
DOI: 10.1128/jvi.00068-24
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.07 Å)
Structure validation

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PDB entries from 2024-11-20

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