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. 2020 Apr 6;11:1713. doi: 10.1038/s41467-020-15575-4

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© The Author(s) 2020

Open Access This 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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 1 — a, b Overall structure, top and side views. The gp20 portal subunits are colored blue and orange and numbered 1 to 12. The S subunits (numbered S1 to S5) and D subunits (numbered D1 to D5) of the major capsid protein gp23* are colored magenta and cyan, respectively. c, d Inter-subunit interactions of the portal assembly. The enlarged inset shows the possible site for inter-subunit disulfide bonding. e, f Structure of gp20 subunit 1. The crown, stem, and clip domains are colored orange, blue, and magenta, respectively. The N-terminal 73 residues and other regions of the wing domain are colored red and green, respectively. The N-whisker region in e has been indicated by a black arrow. g, h Comparison of the in situ gp20 structure with the previously reported recombinantly expressed N-terminal deletion gp20 structure (PDB: 3JA7). The in situ gp20 structure (subunit 1) colored as in e is superimposed on the recombinant gp20 structure colored gray. The bent loop of the recombinant portal structure is shown in black.