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7Z48

Bottom part (C5) of bacteriophage SU10 capsid

Summary for 7Z48
Entry DOI10.2210/pdb7z48/pdb
Related7Z44 7Z45 7Z46 7Z47 7Z49 7Z4A 7Z4B 7Z4F
EMDB information14483 14484 14485 14486 14487 14488 14489 14490 14491 14492 14495
DescriptorMajor head protein (1 entity in total)
Functional Keywordsbacteriophage, portal, virus
Biological sourceEscherichia phage vB_EcoP_SU10
Total number of polymer chains17
Total formula weight656479.77
Authors
Siborova, M.,Fuzik, T.,Prochazkova, M.,Novacek, J.,Plevka, P. (deposition date: 2022-03-03, release date: 2022-08-10, Last modification date: 2024-07-17)
Primary citationSiborova, M.,Fuzik, T.,Prochazkova, M.,Novacek, J.,Benesik, M.,Nilsson, A.S.,Plevka, P.
Tail proteins of phage SU10 reorganize into the nozzle for genome delivery.
Nat Commun, 13:5622-5622, 2022
Cited by
PubMed Abstract: Escherichia coli phage SU10 belongs to the genus Kuravirus from the class Caudoviricetes of phages with short non-contractile tails. In contrast to other short-tailed phages, the tails of Kuraviruses elongate upon cell attachment. Here we show that the virion of SU10 has a prolate head, containing genome and ejection proteins, and a tail, which is formed of portal, adaptor, nozzle, and tail needle proteins and decorated with long and short fibers. The binding of the long tail fibers to the receptors in the outer bacterial membrane induces the straightening of nozzle proteins and rotation of short tail fibers. After the re-arrangement, the nozzle proteins and short tail fibers alternate to form a nozzle that extends the tail by 28 nm. Subsequently, the tail needle detaches from the nozzle proteins and five types of ejection proteins are released from the SU10 head. The nozzle with the putative extension formed by the ejection proteins enables the delivery of the SU10 genome into the bacterial cytoplasm. It is likely that this mechanism of genome delivery, involving the formation of the tail nozzle, is employed by all Kuraviruses.
PubMed: 36153309
DOI: 10.1038/s41467-022-33305-w
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4 Å)
Structure validation

226707

건을2024-10-30부터공개중

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