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7JYI

Subparticle Map of ZIKV MR-766

Summary for 7JYI
Entry DOI10.2210/pdb7jyi/pdb
EMDB information22526 22527
DescriptorE Glycoprotein, M protein (2 entities in total)
Functional Keywordsmr-766 zikv two-fold subparticle, viral protein
Biological sourceZika virus (ZIKV)
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Total number of polymer chains4
Total formula weight125661.68
Authors
Jose, J.,Hafenstein, S. (deposition date: 2020-08-30, release date: 2020-09-16, Last modification date: 2025-05-28)
Primary citationDiNunno, 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: 33009400
DOI: 10.1038/s41467-020-18747-4
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.4 Å)
Structure validation

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