7Z51
Tick-borne encephalitis virus Kuutsalo-14
Summary for 7Z51
Entry DOI | 10.2210/pdb7z51/pdb |
EMDB information | 14512 |
Descriptor | Envelope protein E, Small envelope protein M, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
Functional Keywords | virion, membrane protein, glycoprotein, virus |
Biological source | Tick-borne encephalitis virus (WESTERN SUBTYPE) More |
Total number of polymer chains | 6 |
Total formula weight | 191870.36 |
Authors | Pulkkinen, L.I.A.,Barrass, S.V.,Anastasina, M.,Butcher, S.J. (deposition date: 2022-03-07, release date: 2022-04-20, Last modification date: 2024-10-23) |
Primary citation | Pulkkinen, L.I.A.,Barrass, S.V.,Domanska, A.,Overby, A.K.,Anastasina, M.,Butcher, S.J. Molecular Organisation of Tick-Borne Encephalitis Virus. Viruses, 14:-, 2022 Cited by PubMed Abstract: Tick-borne encephalitis virus (TBEV) is a pathogenic, enveloped, positive-stranded RNA virus in the family . Structural studies of flavivirus virions have primarily focused on mosquito-borne species, with only one cryo-electron microscopy (cryo-EM) structure of a tick-borne species published. Here, we present a 3.3 Å cryo-EM structure of the TBEV virion of the Kuutsalo-14 isolate, confirming the overall organisation of the virus. We observe conformational switching of the peripheral and transmembrane helices of M protein, which can explain the quasi-equivalent packing of the viral proteins and highlights their importance in stabilising membrane protein arrangement in the virion. The residues responsible for M protein interactions are highly conserved in TBEV but not in the structurally studied Hypr strain, nor in mosquito-borne flaviviruses. These interactions may compensate for the lower number of hydrogen bonds between E proteins in TBEV compared to the mosquito-borne flaviviruses. The structure reveals two lipids bound in the E protein which are important for virus assembly. The lipid pockets are comparable to those recently described in mosquito-borne Zika, Spondweni, Dengue, and Usutu viruses. Our results thus advance the understanding of tick-borne flavivirus architecture and virion-stabilising interactions. PubMed: 35458522DOI: 10.3390/v14040792 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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