6EGU

Structure of RVFV envelope protein Gc in postfusion conformation in complex with 1,2-dipropionyl-sn-glycero-3-phosphocholine

Summary for 6EGU

• Entry DOI: 10.2210/pdb6egu/pdb
• Descriptor: RVFV ENVELOPE PROTEIN GC, beta-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: viral fusion envelope glycoprotein bunyavirus phlebovirus, viral protein
• Biological source: Rift Valley fever virus
• Total number of polymer chains: 3
• Total formula weight: 174906.42

Authors

Guardado-Calvo, P.,Rey, F.A. (deposition date: 2017-09-12, release date: 2017-11-01, Last modification date: 2024-10-23)

Primary citation

Guardado-Calvo, P.,Atkovska, K.,Jeffers, S.A.,Grau, N.,Backovic, M.,Perez-Vargas, J.,de Boer, S.M.,Tortorici, M.A.,Pehau-Arnaudet, G.,Lepault, J.,England, P.,Rottier, P.J.,Bosch, B.J.,Hub, J.S.,Rey, F.A.
A glycerophospholipid-specific pocket in the RVFV class II fusion protein drives target membrane insertion.
Science, 358:663-667, 2017

PubMed Abstract: 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.

PubMed: 29097548
DOI: 10.1126/science.aal2712

Experimental method

X-RAY DIFFRACTION (2.3 Å)