7Z46
Top part (C5) of bacteriophage SU10 capsid
Summary for 7Z46
| Entry DOI | 10.2210/pdb7z46/pdb |
| Related | 7Z44 7Z45 7Z47 7Z48 7Z49 7Z4A 7Z4B 7Z4F |
| EMDB information | 14483 14484 14485 14486 14487 14488 14489 14490 14491 14492 14495 |
| Descriptor | Major head protein (1 entity in total) |
| Functional Keywords | bacteriophage, portal, virus |
| Biological source | Escherichia phage vB_EcoP_SU10 |
| Total number of polymer chains | 30 |
| Total formula weight | 1158493.71 |
| Authors | Siborova, M.,Fuzik, T.,Prochazkova, M.,Novacek, J.,Plevka, P. (deposition date: 2022-03-03, release date: 2022-08-24, Last modification date: 2024-07-17) |
| Primary citation | Siborova, 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: 36153309DOI: 10.1038/s41467-022-33305-w PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.4 Å) |
Structure validation
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