6A9S
The crystal structure of vaccinia virus A26 (residues 1-397)
Summary for 6A9S
| Entry DOI | 10.2210/pdb6a9s/pdb |
| Descriptor | Protein A26, 1,2-ETHANEDIOL (3 entities in total) |
| Functional Keywords | vaccinia virus, virus entry, acid sensitive, viral protein |
| Biological source | Vaccinia virus (strain Western Reserve) (VACV) |
| Total number of polymer chains | 1 |
| Total formula weight | 47287.76 |
| Authors | Wang, H.C.,Ko, T.Z.,Luo, Y.C.,Liao, Y.T.,Chang, W. (deposition date: 2018-07-16, release date: 2019-06-12, Last modification date: 2024-11-20) |
| Primary citation | Chang, H.W.,Yang, C.H.,Luo, Y.C.,Su, B.G.,Cheng, H.Y.,Tung, S.Y.,Carillo, K.J.D.,Liao, Y.T.,Tzou, D.M.,Wang, H.C.,Chang, W. Vaccinia viral A26 protein is a fusion suppressor of mature virus and triggers membrane fusion through conformational change at low pH. Plos Pathog., 15:e1007826-e1007826, 2019 Cited by PubMed Abstract: Vaccinia mature virus requires A26 envelope protein to mediate acid-dependent endocytosis into HeLa cells in which we hypothesized that A26 protein functions as an acid-sensitive membrane fusion suppressor. Here, we provide evidence showing that N-terminal domain (aa1-75) of A26 protein is an acid-sensitive region that regulates membrane fusion. Crystal structure of A26 protein revealed that His48 and His53 are in close contact with Lys47, Arg57, His314 and Arg312, suggesting that at low pH these His-cation pairs could initiate conformational changes through protonation of His48 and His53 and subsequent electrostatic repulsion. All the A26 mutant mature viruses that interrupted His-cation pair interactions of His48 and His 53 indeed have lost virion infectivity. Isolation of revertant viruses revealed that second site mutations caused frame shifts and premature termination of A26 protein such that reverent viruses regained cell entry through plasma membrane fusion. Together, we conclude that viral A26 protein functions as an acid-sensitive fusion suppressor during vaccinia mature virus endocytosis. PubMed: 31220181DOI: 10.1371/journal.ppat.1007826 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.18 Å) |
Structure validation
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