8VBX
C6 nozzle and fibre complex of the mature bacteriophage PhiM1 particle
Summary for 8VBX
| Entry DOI | 10.2210/pdb8vbx/pdb |
| Related | 8VB0 8VB2 8VB4 |
| EMDB information | 43109 43110 43111 43112 43127 |
| Descriptor | Tail nozzle (gp51), Tail fiber (gp47) (2 entities in total) |
| Functional Keywords | tail, fiber, fibre, complex, podophage, nozzle, protein, autographiviridae, assembly, viral protein |
| Biological source | Pectobacterium phage PhiM1 More |
| Total number of polymer chains | 24 |
| Total formula weight | 1512194.12 |
| Authors | |
| Primary citation | Eruera, A.R.,Hodgkinson-Bean, J.,Rutter, G.L.,Hills, F.R.,Kumaran, R.,Crowe, A.J.M.,Jadav, N.,Chang, F.,McJarrow-Keller, K.,Jorge, F.,Hyun, J.,Kim, H.,Ryu, B.,Bostina, M. Ejectosome of Pectobacterium bacteriophage Phi M1. Pnas Nexus, 3:pgae416-pgae416, 2024 Cited by PubMed Abstract: Podophages that infect gram-negative bacteria, such as pathogen ΦM1, encode tail assemblies too short to extend across the complex gram-negative cell wall. To overcome this, podophages encode a large protein complex (ejectosome) packaged inside the viral capsid and correspondingly ejected during infection to form a transient channel that spans the periplasmic space. Here, we describe the ejectosome of bacteriophage ΦM1 to a resolution of 3.32 Å by single-particle cryo-electron microscopy (cryo-EM). The core consists of tetrameric and octameric ejection proteins which form a ∼1.5-MDa ejectosome that must transition through the ∼30 Å aperture created by the short tail nozzle assembly that acts as the conduit for the passage of DNA during infection. The ejectosome forms several grooves into which coils of genomic DNA are fit before the DNA sharply turns and goes down the tunnel and into the portal. In addition, we reconstructed the icosahedral capsid and hybrid tail apparatus to resolutions between 3.04 and 3.23 Å, and note an uncommon fold adopted by the dimerized decoration proteins which further emphasize the structural diversity of podophages. These reconstructions have allowed the generation of a complete atomic model of the ΦM1, uncovering two distinct decoration proteins and highlighting the exquisite structural diversity of tailed bacteriophages. PubMed: 39351541DOI: 10.1093/pnasnexus/pgae416 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.23 Å) |
Structure validation
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