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5ZZ8

Structure of the Herpes simplex virus type 2 C-capsid with capsid-vertex-specific component

This is a non-PDB format compatible entry.
Summary for 5ZZ8
Entry DOI10.2210/pdb5zz8/pdb
EMDB information6976
DescriptorVP19C, VP23, Major capsid protein, ... (7 entities in total)
Functional Keywordsherpes simplex virus 2, capsid, capsid-vertex-specific component, structural protein
Biological sourceHuman herpesvirus 2 (HHV-2)
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Total number of polymer chains51
Total formula weight4032164.48
Authors
Wang, J.L.,Yuan, S.,Zhu, D.J.,Tang, H.,Wang, N.,Chen, W.Y.,Gao, Q.,Li, Y.H.,Wang, J.Z.,Liu, H.R.,Zhang, X.Z.,Rao, Z.H.,Wang, X.X. (deposition date: 2018-05-31, release date: 2018-10-10, Last modification date: 2019-11-06)
Primary citationWang, J.,Yuan, S.,Zhu, D.,Tang, H.,Wang, N.,Chen, W.,Gao, Q.,Li, Y.,Wang, J.,Liu, H.,Zhang, X.,Rao, Z.,Wang, X.
Structure of the herpes simplex virus type 2 C-capsid with capsid-vertex-specific component.
Nat Commun, 9:3668-3668, 2018
Cited by
PubMed Abstract: Herpes simplex viruses (HSVs) cause human oral and genital ulcer diseases. Patients with HSV-2 have a higher risk of acquiring a human immunodeficiency virus infection. HSV-2 is a member of the α-herpesvirinae subfamily that together with the β- and γ-herpesvirinae subfamilies forms the Herpesviridae family. Here, we report the cryo-electron microscopy structure of the HSV-2 C-capsid with capsid-vertex-specific component (CVSC) that was determined at 3.75 Å using a block-based reconstruction strategy. We present atomic models of multiple conformers for the capsid proteins (VP5, VP23, VP19C, and VP26) and CVSC. Comparison of the HSV-2 homologs yields information about structural similarities and differences between the three herpesviruses sub-families and we identify α-herpesvirus-specific structural features. The hetero-pentameric CVSC, consisting of a UL17 monomer, a UL25 dimer and a UL36 dimer, is bound tightly by a five-helix bundle that forms extensive networks of subunit contacts with surrounding capsid proteins, which reinforce capsid stability.
PubMed: 30201968
DOI: 10.1038/s41467-018-06078-4
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.75 Å)
Structure validation

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数据于2024-11-06公开中

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