6SP2
CryoEM structure of SERINC from Drosophila melanogaster
Summary for 6SP2
| Entry DOI | 10.2210/pdb6sp2/pdb |
| EMDB information | 10277 10279 |
| Descriptor | Membrane protein TMS1d, Lauryl Maltose Neopentyl Glycol, O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-L-serine, ... (4 entities in total) |
| Functional Keywords | anti-retroviral, tm10, serinc fold, novel fold, membrane protein |
| Biological source | Drosophila melanogaster (Fruit fly) |
| Total number of polymer chains | 6 |
| Total formula weight | 353929.39 |
| Authors | Pye, V.E.,Nans, A.,Cherepanov, P. (deposition date: 2019-08-30, release date: 2020-01-01, Last modification date: 2024-11-06) |
| Primary citation | Pye, V.E.,Rosa, A.,Bertelli, C.,Struwe, W.B.,Maslen, S.L.,Corey, R.,Liko, I.,Hassall, M.,Mattiuzzo, G.,Ballandras-Colas, A.,Nans, A.,Takeuchi, Y.,Stansfeld, P.J.,Skehel, J.M.,Robinson, C.V.,Pizzato, M.,Cherepanov, P. A bipartite structural organization defines the SERINC family of HIV-1 restriction factors. Nat.Struct.Mol.Biol., 27:78-83, 2020 Cited by PubMed Abstract: The human integral membrane protein SERINC5 potently restricts HIV-1 infectivity and sensitizes the virus to antibody-mediated neutralization. Here, using cryo-EM, we determine the structures of human SERINC5 and its orthologue from Drosophila melanogaster at subnanometer and near-atomic resolution, respectively. The structures reveal a novel fold comprised of ten transmembrane helices organized into two subdomains and bisected by a long diagonal helix. A lipid binding groove and clusters of conserved residues highlight potential functional sites. A structure-based mutagenesis scan identified surface-exposed regions and the interface between the subdomains of SERINC5 as critical for HIV-1-restriction activity. The same regions are also important for viral sensitization to neutralizing antibodies, directly linking the antiviral activity of SERINC5 with remodeling of the HIV-1 envelope glycoprotein. PubMed: 31907454DOI: 10.1038/s41594-019-0357-0 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.33 Å) |
Structure validation
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