7JYI
Subparticle Map of ZIKV MR-766
Summary for 7JYI
| Entry DOI | 10.2210/pdb7jyi/pdb |
| EMDB information | 22526 22527 |
| Descriptor | E Glycoprotein, M protein (2 entities in total) |
| Functional Keywords | mr-766 zikv two-fold subparticle, viral protein |
| Biological source | Zika virus (ZIKV) More |
| Total number of polymer chains | 4 |
| Total formula weight | 125661.68 |
| Authors | Jose, J.,Hafenstein, S. (deposition date: 2020-08-30, release date: 2020-09-16, Last modification date: 2025-05-28) |
| Primary citation | DiNunno, N.M.,Goetschius, D.J.,Narayanan, A.,Majowicz, S.A.,Moustafa, I.,Bator, C.M.,Hafenstein, S.L.,Jose, J. Identification of a pocket factor that is critical to Zika virus assembly. Nat Commun, 11:4953-4953, 2020 Cited by PubMed Abstract: Zika virus (ZIKV) is an emerging mosquito borne flavivirus and a major public health concern causing severe disease. Due to the presence of a lipid membrane and structural heterogeneity, attaining an atomic resolution structure is challenging, but important to understand virus assembly and life cycle mechanisms that offer distinct targets for therapeutic intervention. We here use subvolume refinement to achieve a 3.4 Å resolution structure and identify two distinct lipid moieties. The first arises from the inner leaflet and is coordinated by hydrophobic residues of the M and E transmembrane helices that form a binding pocket not previously characterized. The second lipid arises from the outer leaflet coordinate between two E protein helices. Structure-based mutagenesis identifies critical hydrophobic interactions and their effect on the virus life cycle. Results show that lipids play an essential role in the ZIKV assembly pathway revealing a potential target of lipid based antiviral drug development. PubMed: 33009400DOI: 10.1038/s41467-020-18747-4 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.4 Å) |
Structure validation
Download full validation report






