5W7G
An envelope of a filamentous hyperthermophilic virus carries lipids in a horseshoe conformation
Summary for 5W7G
| Entry DOI | 10.2210/pdb5w7g/pdb |
| EMDB information | 8780 |
| Descriptor | ORF140, ORF132, DNA (253-MER) (3 entities in total) |
| Functional Keywords | afv1, hyperthermophile, filamentous virus, a-form dna, virus |
| Biological source | Acidianus filamentous virus 1 (AFV-1) More |
| Total number of polymer chains | 44 |
| Total formula weight | 803345.05 |
| Authors | Kasson, P.,DiMaio, F.,Yu, X.,Lucas-Staat, S.,Krupovic, M.,Schouten, S.,Prangishvili, D.,Egelman, E. (deposition date: 2017-06-19, release date: 2017-07-19, Last modification date: 2024-03-13) |
| Primary citation | Egelman, E.H.,Kasson, P.M.,DiMaio, F.,Yu, X.,Lucas-Staat, S.,Krupovic, M.,Schouten, S.,Prangishvili, D. Model for a novel membrane envelope in a filamentous hyperthermophilic virus. Elife, 6:-, 2017 Cited by PubMed Abstract: Biological membranes create compartments, and are usually formed by lipid bilayers. However, in hyperthermophilic archaea that live optimally at temperatures above 80°C the membranes are monolayers which resemble fused bilayers. Many double-stranded DNA viruses which parasitize such hosts, including the filamentous virus AFV1 of , are enveloped with a lipid-containing membrane. Using cryo-EM, we show that the membrane in AFV1 is a ~2 nm-thick monolayer, approximately half the expected membrane thickness, formed by host membrane-derived lipids which adopt a U-shaped 'horseshoe' conformation. We hypothesize that this unusual viral envelope structure results from the extreme curvature of the viral capsid, as 'horseshoe' lipid conformations favor such curvature and host membrane lipids that permit horseshoe conformations are selectively recruited into the viral envelope. The unusual envelope found in AFV1 also has many implications for biotechnology, since this membrane can survive the most aggressive conditions involving extremes of temperature and pH. PubMed: 28639939DOI: 10.7554/eLife.26268 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.5 Å) |
Structure validation
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