8INI

vaccinia H2 protein without the transmembrane region

Summary for 8INI

• Entry DOI: 10.2210/pdb8ini/pdb
• Descriptor: vaccinia h2 protein, TETRAETHYLENE GLYCOL (3 entities in total)
• Functional Keywords: membrane fusion, entry component, viral protein
• Biological source: Vaccinia virus
• Total number of polymer chains: 2
• Total formula weight: 22804.13

Authors

Liu, C.Y.,Ko, T.P.,Wang, H.C.,Chang, W. (deposition date: 2023-03-10, release date: 2023-11-15, Last modification date: 2024-10-23)

Primary citation

Kao, C.F.,Liu, C.Y.,Hsieh, C.L.,Carillo, K.J.D.,Tzou, D.L.M.,Wang, H.C.,Chang, W.
Structural and functional analyses of viral H2 protein of the vaccinia virus entry fusion complex.
J.Virol., 97:e0134323-e0134323, 2023

PubMed Abstract: Vaccinia virus infection requires virus-cell membrane fusion to complete entry during endocytosis; however, it contains a large viral fusion protein complex of 11 viral proteins that share no structure or sequence homology to all the known viral fusion proteins, including type I, II, and III fusion proteins. It is thus very challenging to investigate how the vaccinia fusion complex works to trigger membrane fusion with host cells. In this study, we crystallized the ectodomain of vaccinia H2 protein, one component of the viral fusion complex. Furthermore, we performed a series of mutational, biochemical, and molecular analyses and identified two surface loops containing LGYSG and RRGTGDAW as the A28-binding region. We also showed that residues in the N-terminal helical region (amino acids 51-90) are also important for H2 function.

PubMed: 37975688
DOI: 10.1128/jvi.01343-23

Experimental method

X-RAY DIFFRACTION (1.75 Å)