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Herpes simplex virus (HSV)\u22121 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 trans-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\u2013like 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.<\/jats:p>","DOI":"10.7554\/elife.53789","type":"journal-article","created":{"date-parts":[[2020,5,11]],"date-time":"2020-05-11T08:00:28Z","timestamp":1589184028000},"update-policy":"https:\/\/doi.org\/10.7554\/elife.53789","source":"Crossref","is-referenced-by-count":44,"title":["Insights into herpesvirus assembly from the structure of the pUL7:pUL51 complex"],"prefix":"10.7554","volume":"9","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-6718-0470","authenticated-orcid":true,"given":"Benjamin G","family":"Butt","sequence":"first","affiliation":[{"name":"Department of Pathology, University of Cambridge, Cambridge, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Danielle J","family":"Owen","sequence":"additional","affiliation":[{"name":"Department of Pathology, University of Cambridge, Cambridge, United 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