Structural highlights
3p54 is a 1 chain structure with sequence from Japanese encephalitis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Related: | 2i69, 2hg0, 1uzg, 1oke, 1tg8, 1svb, 2ala |
| Gene: | Envelope protein E (Japanese encephalitis) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[Q99DQ9_9FLAV] Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes (By similarity).[SAAS:SAAS026470_004_099774]
Publication Abstract from PubMed
Japanese Encephalitis Virus (JEV) is the leading global cause of viral encephalitis. The JEV envelope protein (E) facilitates cellular attachment and membrane fusion and is the primary target of neutralizing antibodies. Herein, we have determined the 2.1A resolution crystal structure of the JEV E ectodomain refolded from bacterial inclusion bodies. The E protein possesses the three domains characteristic of flavivirus envelopes and epitope mapping of neutralizing antibodies onto the structure reveals determinants that correspond to the domain I lateral ridge, fusion loop, domain III lateral ridge and domain I-II hinge. While monomeric in solution, JEV E assembles as an antiparallel dimer in the crystal lattice organized in a highly similar fashion as seen in cryoEM models of mature flavivirus virions. The dimer interface, however, is remarkably small and lacks many of the domain II contacts observed in other flavivirus E homodimers. Additionally, uniquely conserved histidines within the JEV serocomplex suggest that pH mediated structural transitions may be aided by lateral interactions outside the dimer interface in the icosahedral virion. Our results suggest that variation of dimer structure and stability may significantly influence the assembly, receptor interaction and uncoating of virions.
Crystal structure of the Japanese encephalitis virus envelope protein.,Luca VC, Abimansour J, Nelson CA, Fremont DH J Virol. 2011 Dec 7. PMID:22156523[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Luca VC, Abimansour J, Nelson CA, Fremont DH. Crystal structure of the Japanese encephalitis virus envelope protein. J Virol. 2011 Dec 7. PMID:22156523 doi:10.1128/JVI.06072-11
