6T5A

Crystal structure of herpes simplex virus 1 pUL7:pUL51 complex

Summary for 6T5A

• Entry DOI: 10.2210/pdb6t5a/pdb
• Descriptor: Tegument protein UL51, Cytoplasmic envelopment protein 1, GLYCEROL, ... (5 entities in total)
• Functional Keywords: custard, assembly, tegument, hsv-1, viral protein
• Biological source: Human herpesvirus 1 (Herpes simplex virus type 1); More
• Total number of polymer chains: 8
• Total formula weight: 195610.58

Authors

Butt, B.G.,Graham, S.C. (deposition date: 2019-10-15, release date: 2020-05-20, Last modification date: 2024-05-15)

Primary citation

Butt, B.G.,Owen, D.J.,Jeffries, C.M.,Ivanova, L.,Hill, C.H.,Houghton, J.W.,Ahmed, M.F.,Antrobus, R.,Svergun, D.I.,Welch, J.J.,Crump, C.M.,Graham, S.C.
Insights into herpesvirus assembly from the structure of the pUL7:pUL51 complex.
Elife, 9:-, 2020

PubMed Abstract: Herpesviruses acquire their membrane envelopes in the cytoplasm of infected cells via a molecular mechanism that remains unclear. Herpes simplex virus (HSV)-1 proteins pUL7 and pUL51 form a complex required for efficient virus envelopment. We show that interaction between homologues of pUL7 and pUL51 is conserved across human herpesviruses, as is their association with -Golgi membranes. We characterized the HSV-1 pUL7:pUL51 complex by solution scattering and chemical crosslinking, revealing a 1:2 complex that can form higher-order oligomers in solution, and we solved the crystal structure of the core pUL7:pUL51 heterodimer. While pUL7 adopts a previously-unseen compact fold, the helix-turn-helix conformation of pUL51 resembles the cellular endosomal complex required for transport (ESCRT)-III component CHMP4B and pUL51 forms ESCRT-III-like filaments, suggesting a direct role for pUL51 in promoting membrane scission during virus assembly. Our results provide a structural framework for understanding the role of the conserved pUL7:pUL51 complex in herpesvirus assembly.

PubMed: 32391791
DOI: 10.7554/eLife.53789

Experimental method

X-RAY DIFFRACTION (1.83 Å)