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. 2020 Apr 23;11(5):339–351. doi: 10.1007/s13238-020-00710-0

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© The Author(s) 2020

Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Characterization and overall structure of the hexameric terminase assembly. (A) Model for herpesvirus procapsid during DNA packaging. (B) Characterization of the terminase complex analyzed by analytical ultracentrifugation, SDS-PAGE and electron microscopy. (C) Representative curves of the MESG-based assays to measure the ATPase activities of wild-type and R346A mutant hexameric terminase rings and wild-type monomer terminase complex. (D) CryoEM map of the hexameric terminase assembly. The inset shows the blocked-based reconstruction for one terminase complex, which consists of pUL15 (blue), pUL28 (green) and pUL33 (magenta). (E and F) Atomic models for the hexameric terminase assembly and the terminase complex. Color scheme is the same as Fig. 1D