7qog | pdb_00007qog

Portal protein assembly of the phicrAss001 virion with C12 symmetry imposed

spinqualitylabelsall models 7qog, resolution 3.09Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7qog is a 5 chain structure with sequence from CrAss-like viruses. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.09Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PORTL_BPCA1 Forms the portal vertex of the capsid (PubMed:37138077). Probably involved in head assembly, genome packaging, tail attachment, and genome ejection (Probable). Publication Abstract from PubMed CrAssphage and related viruses of the order Crassvirales (hereafter referred to as crassviruses) were originally discovered by cross-assembly of metagenomic sequences. They are the most abundant viruses in the human gut, are found in the majority of individual gut viromes, and account for up to 95% of the viral sequences in some individuals(1-4). Crassviruses are likely to have major roles in shaping the composition and functionality of the human microbiome, but the structures and roles of most of the virally encoded proteins are unknown, with only generic predictions resulting from bioinformatic analyses(4,5). Here we present a cryo-electron microscopy reconstruction of Bacteroides intestinalis virus PhicrAss001(6), providing the structural basis for the functional assignment of most of its virion proteins. The muzzle protein forms an assembly about 1 MDa in size at the end of the tail and exhibits a previously unknown fold that we designate the 'crass fold', that is likely to serve as a gatekeeper that controls the ejection of cargos. In addition to packing the approximately 103 kb of virus DNA, the PhicrAss001 virion has extensive storage space for virally encoded cargo proteins in the capsid and, unusually, within the tail. One of the cargo proteins is present in both the capsid and the tail, suggesting a general mechanism for protein ejection, which involves partial unfolding of proteins during their extrusion through the tail. These findings provide a structural basis for understanding the mechanisms of assembly and infection of these highly abundant crassviruses. Structural atlas of a human gut crassvirus.,Bayfield OW, Shkoporov AN, Yutin N, Khokhlova EV, Smith JLR, Hawkins DEDP, Koonin EV, Hill C, Antson AA Nature. 2023 May;617(7960):409-416. doi: 10.1038/s41586-023-06019-2. Epub 2023 , May 3. PMID:37138077 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Portal protein 3D structures

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