6CGR

CryoEM structure of herpes simplex virus 1 capsid with associated tegument protein complexes.

This is a non-PDB format compatible entry.

Summary for 6CGR

• Entry DOI: 10.2210/pdb6cgr/pdb
• EMDB information: 7472
• Descriptor: Major capsid protein, Small capsomere-interacting protein, Triplex capsid protein 1, ... (7 entities in total)
• Functional Keywords: human herpesvirus 1, herpes simplex virus type 1, capsid-associated tegument complex, virus
• Biological source: Human herpesvirus 1 (HHV-1); More
• Total number of polymer chains: 51
• Total formula weight: 4031743.96

Authors

Dai, X.H.,Zhou, Z.H. (deposition date: 2018-02-20, release date: 2018-03-14, Last modification date: 2019-11-27)

Primary citation

Dai, X.,Zhou, Z.H.
Structure of the herpes simplex virus 1 capsid with associated tegument protein complexes.
Science, 360:-, 2018

PubMed Abstract: Herpes simplex viruses (HSVs) rely on capsid-associated tegument complex (CATC) for long-range axonal transport of their genome-containing capsids between sites of infection and neuronal cell bodies. Here we report cryo-electron microscopy structures of the HSV-1 capsid with CATC up to 3.5-angstrom resolution and atomic models of multiple conformers of capsid proteins VP5, VP19c, VP23, and VP26 and tegument proteins pUL17, pUL25, and pUL36. Crowning every capsid vertex are five copies of heteropentameric CATC, each containing a pUL17 monomer supporting the coiled-coil helix bundle of a pUL25 dimer and a pUL36 dimer, thus positioning their flexible domains for potential involvement in nuclear capsid egress and axonal capsid transport. Notwithstanding newly discovered fold conservation between triplex proteins and bacteriophage λ protein gpD and the previously recognized bacteriophage HK97 gp5-like fold in VP5, HSV-1 capsid proteins exhibit extraordinary diversity in forms of domain insertion and conformational polymorphism, not only for interactions with tegument proteins but also for encapsulation of large genomes.

PubMed: 29622628
DOI: 10.1126/science.aao7298

Experimental method

ELECTRON MICROSCOPY (4.2 Å)