5ZAP

Atomic structure of the herpes simplex virus type 2 B-capsid

This is a non-PDB format compatible entry.

Summary for 5ZAP

• Entry DOI: 10.2210/pdb5zap/pdb
• EMDB information: 6907
• Descriptor: Major capsid protein, Triplex capsid protein 2, Triplex capsid protein 1, ... (4 entities in total)
• Functional Keywords: herpesvirus, capsid, cryo-em, atomic structure, virus
• Biological source: Human herpesvirus 2 (HHV-2); More
• Total number of polymer chains: 46
• Total formula weight: 3168592.28

Authors

Yuan, S.,Wang, J.L.,Zhu, D.J.,Wang, N.,Gao, Q.,Chen, W.Y.,Tang, H.,Wang, J.Z.,Zhang, X.Z.,Liu, H.R.,Rao, Z.H.,Wang, X.X. (deposition date: 2018-02-08, release date: 2018-04-18, Last modification date: 2024-10-09)

Primary citation

Yuan, S.,Wang, J.L.,Zhu, D.J.,Wang, N.,Gao, Q.,Chen, W.Y.,Tang, H.,Wang, J.Z.,Zhang, X.Z.,Liu, H.R.,Rao, Z.H.,Wang, X.X.
Cryo-EM structure of a herpesvirus capsid at 3.1 angstrom.
Science, 360:-, 2018

PubMed Abstract: Structurally and genetically, human herpesviruses are among the largest and most complex of viruses. Using cryo-electron microscopy (cryo-EM) with an optimized image reconstruction strategy, we report the herpes simplex virus type 2 (HSV-2) capsid structure at 3.1 angstroms, which is built up of about 3000 proteins organized into three types of hexons (central, peripentonal, and edge), pentons, and triplexes. Both hexons and pentons contain the major capsid protein, VP5; hexons also contain a small capsid protein, VP26; and triplexes comprise VP23 and VP19C. Acting as core organizers, VP5 proteins form extensive intermolecular networks, involving multiple disulfide bonds (about 1500 in total) and noncovalent interactions, with VP26 proteins and triplexes that underpin capsid stability and assembly. Conformational adaptations of these proteins induced by their microenvironments lead to 46 different conformers that assemble into a massive quasisymmetric shell, exemplifying the structural and functional complexity of HSV.

PubMed: 29622627
DOI: 10.1126/science.aao7283

Experimental method

ELECTRON MICROSCOPY (3.1 Å)