{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Mirzakhanyan Y"],"funding":["HHS | National Institutes of Health","NIH HHS","NIGMS NIH HHS"],"pubmed_abstract":["Vaccinia virus, the prototypical poxvirus and smallpox/monkeypox vaccine, has proven a challenging entity for structural biology, defying many of the approaches leading to molecular and atomic models for other viruses. Via a combination of deep learning and cross-linking mass spectrometry, we have developed an atomic-level model and an integrated processing/assembly pathway for a structural component of the vaccinia virion, protein P4a. Within the pathway, proteolytic separation of the C-terminal P4a-3 segment of P4a triggers a massive conformational rotation within the N-terminal P4a-1 segment that becomes fixed by disulfide-locking while removing a steric block to trimerization of the processing intermediate P4a-1+2. These events trigger the proteolytic separation of P4a-2, allowing the "],"journal":["mBio"],"pagination":["e0113523"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10653903"],"repository":["biostudies-literature"],"pubmed_title":["Combination of deep XLMS with deep learning reveals an ordered rearrangement and assembly of a major protein component of the vaccinia virion."],"pmcid":["PMC10653903"],"funding_grant_id":["1R01GM134144-01","S10 OD016328","R01 GM134144"],"pubmed_authors":["Mirzakhanyan Y","Jankevics A","Gershon PD","Scheltema RA"],"additional_accession":[]},"is_claimable":false,"name":"Combination of deep XLMS with deep learning reveals an ordered rearrangement and assembly of a major protein component of the vaccinia virion.","description":"Vaccinia virus, the prototypical poxvirus and smallpox/monkeypox vaccine, has proven a challenging entity for structural biology, defying many of the approaches leading to molecular and atomic models for other viruses. Via a combination of deep learning and cross-linking mass spectrometry, we have developed an atomic-level model and an integrated processing/assembly pathway for a structural component of the vaccinia virion, protein P4a. Within the pathway, proteolytic separation of the C-terminal P4a-3 segment of P4a triggers a massive conformational rotation within the N-terminal P4a-1 segment that becomes fixed by disulfide-locking while removing a steric block to trimerization of the processing intermediate P4a-1+2. These events trigger the proteolytic separation of P4a-2, allowing the ","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Aug","modification":"2025-04-03T22:05:45.707Z","creation":"2024-10-15T11:03:09.773Z"},"accession":"S-EPMC10653903","cross_references":{"pubmed":["37646531"],"doi":["10.1128/mbio.01135-23"]}}