6egt | pdb_00006egt

Structure of RVFV envelope protein Gc in postfusion conformation in complex with MES

spinqualitylabelsall models 6egt, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6egt is a 3 chain structure with sequence from Rvfv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FUL, MES, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The Rift Valley fever virus (RVFV) is transmitted by infected mosquitoes, causing severe disease in humans and livestock across Africa. We determined the x-ray structure of the RVFV class II fusion protein Gc in its postfusion form and in complex with a glycerophospholipid (GPL) bound in a conserved cavity next to the fusion loop. Site-directed mutagenesis and molecular dynamics simulations further revealed a built-in motif allowing en bloc insertion of the fusion loop into membranes, making few nonpolar side-chain interactions with the aliphatic moiety and multiple polar interactions with lipid head groups upon membrane restructuring. The GPL head-group recognition pocket is conserved in the fusion proteins of other arthropod-borne viruses, such as Zika and chikungunya viruses, which have recently caused major epidemics worldwide. A glycerophospholipid-specific pocket in the RVFV class II fusion protein drives target membrane insertion.,Guardado-Calvo P, Atkovska K, Jeffers SA, Grau N, Backovic M, Perez-Vargas J, de Boer SM, Tortorici MA, Pehau-Arnaudet G, Lepault J, England P, Rottier PJ, Bosch BJ, Hub JS, Rey FA Science. 2017 Nov 3;358(6363):663-667. doi: 10.1126/science.aal2712. PMID:29097548 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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