5mdm | pdb_00005mdm

Structural intermediates in the fusion associated transition of vesiculovirus glycoprotein

spinqualitylabelsall models 5mdm, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5mdm is a 4 chain structure with sequence from Chandipura virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NAG, SO4, FUC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [GLYCO_CHAV] Attaches the virus to host cellular receptor, inducing endocytosis of the virion. In the endosome, the acidic pH induces conformational changes in the glycoprotein trimer, which trigger fusion between virus and cell membrane (By similarity). Publication Abstract from PubMed Vesiculoviruses enter cells by membrane fusion, driven by a large, low-pH-induced, conformational change in the fusion glycoprotein G that involves transition from a trimeric pre-fusion toward a trimeric post-fusion state via monomeric intermediates. Here, we present the structure of the G fusion protein at intermediate pH for two vesiculoviruses, vesicular stomatitis virus (VSV) and Chandipura virus (CHAV), which is responsible for deadly encephalopathies. First, a CHAV G crystal structure shows two intermediate conformations forming a flat dimer of heterodimers. On virions, electron microscopy (EM) and tomography reveal monomeric spikes similar to one of the crystal conformations. In solution, mass spectrometry shows dimers of G. Finally, mutations at a dimer interface, involving fusion domains associated in an antiparallel manner to form an intermolecular beta-sheet, affect G fusion properties. The location of the compensatory mutations restoring fusion activity strongly suggests that this interface is functionally relevant. This work reveals the range of G structural changes and suggests that G monomers can re-associate, through antiparallel interactions between fusion domains, into dimers that play a role at some early stage of the fusion process. Structural intermediates in the fusion-associated transition of vesiculovirus glycoprotein.,Baquero E, Albertini AA, Raux H, Abou-Hamdan A, Boeri-Erba E, Ouldali M, Buonocore L, Rose JK, Lepault J, Bressanelli S, Gaudin Y EMBO J. 2017 Mar 1;36(5):679-692. doi: 10.15252/embj.201694565. Epub 2017 Feb 10. PMID:28188244 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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