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6CJ6

Structure of the poxvirus protein F9

Summary for 6CJ6
Entry DOI10.2210/pdb6cj6/pdb
DescriptorProtein F9, S-1,2-PROPANEDIOL, 2-ETHOXYETHANOL, ... (16 entities in total)
Functional Keywordsentry fusion complex associated protein, viral protein
Biological sourceVaccinia virus (strain Western Reserve) (VACV)
Total number of polymer chains4
Total formula weight92217.32
Authors
Diesterbeck, U.S.,Gittis, A.G.,Garboczi, D.N.,Moss, B. (deposition date: 2018-02-26, release date: 2019-03-06, Last modification date: 2024-10-23)
Primary citationDiesterbeck, U.S.,Gittis, A.G.,Garboczi, D.N.,Moss, B.
The 2.1 angstrom structure of protein F9 and its comparison to L1, two components of the conserved poxvirus entry-fusion complex.
Sci Rep, 8:16807-16807, 2018
Cited by
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 genome to contain the most distantly related F9 and L1 sequences compared to the vaccinia proteins studied here. The structural differences between F9 and L1 suggest functional adaptations during evolution from a common precursor that underlie the present requirement for each protein.
PubMed: 30429486
DOI: 10.1038/s41598-018-34244-7
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

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