8vb4 | pdb_00008vb4

C12 portal and adaptor complex of the mature bacteriophage PhiM1 particle

spinqualitylabelsall models 8vb4, resolution 2.98Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8vb4 is a 24 chain structure with sequence from Pectobacterium phage PhiM1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.98Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A1P7WG10_9CAUD Forms the portal vertex of the capsid. This portal plays critical roles in head assembly, genome packaging, neck/tail attachment, and genome ejection. The portal protein multimerizes as a single ring-shaped homododecamer arranged around a central channel.[ARBA:ARBA00003421] Publication Abstract from PubMed Podophages that infect gram-negative bacteria, such as Pectobacterium pathogen PhiM1, 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 PhiM1 to a resolution of 3.32 A by single-particle cryo-electron microscopy (cryo-EM). The core consists of tetrameric and octameric ejection proteins which form a approximately 1.5-MDa ejectosome that must transition through the approximately 30 A 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 A, 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 PhiM1, uncovering two distinct decoration proteins and highlighting the exquisite structural diversity of tailed bacteriophages. Ejectosome of Pectobacterium bacteriophage PhiM1.,Eruera AR, Hodgkinson-Bean J, Rutter GL, Hills FR, Kumaran R, Crowe AJM, Jadav N, Chang F, McJarrow-Keller K, Jorge F, Hyun J, Kim H, Ryu B, Bostina M PNAS Nexus. 2024 Sep 19;3(9):pgae416. doi: 10.1093/pnasnexus/pgae416. eCollection , 2024 Sep. PMID:39351541 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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