{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["8(1)"],"submitter":["Diesterbeck US"],"pubmed_abstract":["The poxvirus F9 protein is a component of the vaccinia virus entry fusion complex (EFC) which consists of 11 proteins. The EFC forms a unique apparatus among viral fusion proteins and complexes. We solved the atomic structure of the F9 ectodomain at 2.10 Å. A structural comparison to the ectodomain of the EFC protein L1 indicated a similar fold and organization, in which a bundle of five α-helices is packed against two pairs of β-strands. However, instead of the L1 myristoylation site and hydrophobic cavity, F9 possesses a protruding loop between α-helices α3 and α4 starting at Gly90. Gly90 is conserved in all poxviruses except Salmon gill poxvirus (SGPV) and Diachasmimorpha longicaudata entomopoxvirus. Phylogenetic sequence analysis of all Poxviridae F9 and L1 orthologs revealed the SGPV "],"journal":["Scientific reports"],"pagination":["16807"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6235832"],"repository":["biostudies-literature"],"pubmed_title":["The 2.1 A structure of protein F9 and its comparison to L1, two components of the conserved poxvirus entry-fusion complex."],"pmcid":["PMC6235832"],"pubmed_authors":["Diesterbeck US","Moss B","Garboczi DN","Gittis AG"],"additional_accession":[]},"is_claimable":false,"name":"The 2.1 A structure of protein F9 and its comparison to L1, two components of the conserved poxvirus entry-fusion complex.","description":"The poxvirus F9 protein is a component of the vaccinia virus entry fusion complex (EFC) which consists of 11 proteins. The EFC forms a unique apparatus among viral fusion proteins and complexes. We solved the atomic structure of the F9 ectodomain at 2.10 Å. A structural comparison to the ectodomain of the EFC protein L1 indicated a similar fold and organization, in which a bundle of five α-helices is packed against two pairs of β-strands. However, instead of the L1 myristoylation site and hydrophobic cavity, F9 possesses a protruding loop between α-helices α3 and α4 starting at Gly90. Gly90 is conserved in all poxviruses except Salmon gill poxvirus (SGPV) and Diachasmimorpha longicaudata entomopoxvirus. Phylogenetic sequence analysis of all Poxviridae F9 and L1 orthologs revealed the SGPV ","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Nov","modification":"2026-05-06T02:33:53.357Z","creation":"2019-03-27T00:08:42Z"},"accession":"S-EPMC6235832","cross_references":{"pubmed":["30429486"],"doi":["10.1038/s41598-018-34244-7"]}}