5ZKX
The postfusion structure of human-infecting Bourbon virus envelope glycoprotein
Summary for 5ZKX
| Entry DOI | 10.2210/pdb5zkx/pdb |
| Descriptor | Envelope glycoprotein (2 entities in total) |
| Functional Keywords | bouv, glycoprotein, viral protein |
| Biological source | Bourbon virus |
| Total number of polymer chains | 3 |
| Total formula weight | 158794.88 |
| Authors | Qi, J.X.,Wu, Y.,Peng, R.C.,Gao, F. (deposition date: 2018-03-26, release date: 2019-03-27, Last modification date: 2024-11-13) |
| Primary citation | Bai, C.,Qi, J.,Wu, Y.,Wang, X.,Gao, G.F.,Peng, R.,Gao, F. Postfusion structure of human-infecting Bourbon virus envelope glycoprotein. J.Struct.Biol., 208:99-106, 2019 Cited by PubMed Abstract: Thogotoviruses are important zoonotic viruses infecting a variety of domestic animals, as well as humans. Among these viruses, Bourbon virus (BRBV) is one of the several human-infecting members, which emerged in the US in recent years and caused human deaths. Here, we report the crystal structure of the BRBV envelope glycoprotein in the postfusion conformation. The structure adopts the typical fold of a class III viral fusion protein and displays an extensive positively charged electrostatic potential pattern, which resembles the glycoprotein of Dhori virus and is consistent with our previous predictions. In addition, compared to other previously defined class III viral fusion proteins, the structures of all thogotovirus glycoproteins and homologs are more similar to herpes virus glycoprotein Bs than to the rhabdovirus G proteins. Thus, class III viral fusion proteins are quite diverse in structure, and sub-classes may have developed during evolution. PubMed: 31419524DOI: 10.1016/j.jsb.2019.08.005 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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