{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["12(3)"],"submitter":["Lin CS"],"pubmed_abstract":["Membrane fusion is essential for viral entry. Unlike class I-III fusion proteins, vaccinia virus (VACV) uses a multicomponent entry fusion complex (EFC). Using cryo-electron microscopy, we determined the full-length structure of the VACV EFC at near-atomic resolution, revealing a 15-protein asymmetric assembly organized into three layers. The central A16/G9/J5 heterotrimer forms the fusion core, stabilized by conserved PXXCW and Delta motifs, and anchors two A28/H2 adaptor dimers linked to peripheral G3/L5/A21/O3 scaffolds. Structural and evolutionary analyses identify a conserved N-terminal domain in A16 containing a myristoyl-binding pocket and a phenylalanine-rich region that stabilizes the trimer and may regulate lipid engagement. An additional component, F9, binds peripherally to J5, "],"journal":["Science advances"],"pagination":["eaec0254"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12802840"],"repository":["biostudies-literature"],"pubmed_title":["Cryo-EM structure of the vaccinia virus entry fusion complex reveals a multicomponent fusion machinery."],"pmcid":["PMC12802840"],"pubmed_authors":["Wang CH","Yeh MC","Lee HM","Lin CS","Gao HD","Ho MC","Chiu HJ","Li CA","Kao CF","Chang W"],"additional_accession":[]},"is_claimable":false,"name":"Cryo-EM structure of the vaccinia virus entry fusion complex reveals a multicomponent fusion machinery.","description":"Membrane fusion is essential for viral entry. Unlike class I-III fusion proteins, vaccinia virus (VACV) uses a multicomponent entry fusion complex (EFC). Using cryo-electron microscopy, we determined the full-length structure of the VACV EFC at near-atomic resolution, revealing a 15-protein asymmetric assembly organized into three layers. The central A16/G9/J5 heterotrimer forms the fusion core, stabilized by conserved PXXCW and Delta motifs, and anchors two A28/H2 adaptor dimers linked to peripheral G3/L5/A21/O3 scaffolds. Structural and evolutionary analyses identify a conserved N-terminal domain in A16 containing a myristoyl-binding pocket and a phenylalanine-rich region that stabilizes the trimer and may regulate lipid engagement. An additional component, F9, binds peripherally to J5, ","dates":{"release":"2026-01-01T00:00:00Z","publication":"2026 Jan","modification":"2026-06-06T13:16:13.518Z","creation":"2026-05-31T03:07:09.019Z"},"accession":"S-EPMC12802840","cross_references":{"pubmed":["41533782"],"doi":["10.1126/sciadv.aec0254"]}}