7A4A
Envelope glycprotein of endogenous retrovirus Y032 (Atlas virus) from the human hookworm Ancylostoma ceylanicum
Summary for 7A4A
Entry DOI | 10.2210/pdb7a4a/pdb |
EMDB information | 11630 |
Descriptor | Integrase catalytic domain-containing protein, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total) |
Functional Keywords | class ii membrane fusion protein; retroviral envelope protein (env); lipid binding protein; disulfide bonding, viral protein |
Biological source | Ancylostoma ceylanicum |
Total number of polymer chains | 3 |
Total formula weight | 155220.89 |
Authors | Mata, C.P.,Merchant, M.,Modis, Y. (deposition date: 2020-08-19, release date: 2021-09-01, Last modification date: 2024-10-16) |
Primary citation | Merchant, M.,Mata, C.P.,Liu, Y.,Zhai, H.,Protasio, A.V.,Modis, Y. A bioactive phlebovirus-like envelope protein in a hookworm endogenous virus. Sci Adv, 8:eabj6894-eabj6894, 2022 Cited by PubMed Abstract: Endogenous viral elements (EVEs), accounting for 15% of our genome, serve as a genetic reservoir from which new genes can emerge. Nematode EVEs are particularly diverse and informative of virus evolution. We identify Atlas virus-an intact retrovirus-like EVE in the human hookworm , with an envelope protein genetically related to G-G glycoproteins from the family Phenuiviridae. A cryo-EM structure of Atlas G reveals a class II viral membrane fusion protein fold not previously seen in retroviruses. Atlas G has the structural hallmarks of an active fusogen. Atlas G trimers insert into membranes with endosomal lipid compositions and low pH. When expressed on the plasma membrane, Atlas G has cell-cell fusion activity. With its preserved biological activities, Atlas G has the potential to acquire a cellular function. Our work reveals structural plasticity in reverse-transcribing RNA viruses. PubMed: 35544562DOI: 10.1126/sciadv.abj6894 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.76 Å) |
Structure validation
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