6qgi

Crystal structure of VP5 from Haloarchaeal pleomorphic virus 2

spinqualitylabelsall models 6qgi, resolution 2.46Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6qgi is a 1 chain structure with sequence from Halorubrum pleomorphic virus 2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.46Å Ligands: CL, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function H9ABL9_9VIRU Publication Abstract from PubMed Lipid membrane fusion is an essential function in many biological processes. Detailed mechanisms of membrane fusion and the protein structures involved have been mainly studied in eukaryotic systems, whereas very little is known about membrane fusion in prokaryotes. Haloarchaeal pleomorphic viruses (HRPVs) have a membrane envelope decorated with spikes that are presumed to be responsible for host attachment and membrane fusion. Here we determine atomic structures of the ectodomains of the 57-kDa spike protein VP5 from two related HRPVs revealing a previously unreported V-shaped fold. By Volta phase plate cryo-electron tomography we show that VP5 is monomeric on the viral surface, and we establish the orientation of the molecules with respect to the viral membrane. We also show that the viral membrane fuses with the host cytoplasmic membrane in a process mediated by VP5. This sheds light on protein structures involved in prokaryotic membrane fusion. The structure of a prokaryotic viral envelope protein expands the landscape of membrane fusion proteins.,El Omari K, Li S, Kotecha A, Walter TS, Bignon EA, Harlos K, Somerharju P, De Haas F, Clare DK, Molin M, Hurtado F, Li M, Grimes JM, Bamford DH, Tischler ND, Huiskonen JT, Stuart DI, Roine E Nat Commun. 2019 Feb 19;10(1):846. doi: 10.1038/s41467-019-08728-7. PMID:30783086 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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