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6XF7

SLP

Summary for 6XF7
Entry DOI10.2210/pdb6xf7/pdb
EMDB information22165
DescriptorLambda 1 protein (1 entity in total)
Functional Keywordsvirus like particle
Biological sourceMammalian orthoreovirus
Total number of polymer chains2
Total formula weight238041.12
Authors
Sutton, G.,Sun, D.P.,Fu, X.F.,Kotecha, A.,Hecksel, G.W.,Clare, D.K.,Zhang, P.,Stuart, D.,Boyce, M. (deposition date: 2020-06-15, release date: 2020-09-23, Last modification date: 2024-03-06)
Primary citationSutton, G.,Sun, D.,Fu, X.,Kotecha, A.,Hecksel, C.W.,Clare, D.K.,Zhang, P.,Stuart, D.I.,Boyce, M.
Assembly intermediates of orthoreovirus captured in the cell.
Nat Commun, 11:4445-4445, 2020
Cited by
PubMed Abstract: Traditionally, molecular assembly pathways for viruses are inferred from high resolution structures of purified stable intermediates, low resolution images of cell sections and genetic approaches. Here, we directly visualise an unsuspected 'single shelled' intermediate for a mammalian orthoreovirus in cryo-preserved infected cells, by cryo-electron tomography of cellular lamellae. Particle classification and averaging yields structures to 5.6 Å resolution, sufficient to identify secondary structural elements and produce an atomic model of the intermediate, comprising 120 copies each of protein λ1 and σ2. This λ1 shell is 'collapsed' compared to the mature virions, with molecules pushed inwards at the icosahedral fivefolds by ~100 Å, reminiscent of the first assembly intermediate of certain prokaryotic dsRNA viruses. This supports the supposition that these viruses share a common ancestor, and suggests mechanisms for the assembly of viruses of the Reoviridae. Such methodology holds promise for dissecting the replication cycle of many viruses.
PubMed: 32895380
DOI: 10.1038/s41467-020-18243-9
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (6.6 Å)
Structure validation

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