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. 2020 Jan 31;11:632. doi: 10.1038/s41467-020-14377-y

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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 Two different structures (FKL and E/Q) of the full-length rA3G (Supplementary Fig. 1 for 2nd structure assignment), showing that CD1 of both structures has a typical APOBEC fold with a Zn (sphere) at the active center. However, CD2 differs in the two structures. The CD2 of the FKL (A) has a canonical CD2 fold, but the CD2 of E/Q (B) re-folds helix 2 (h2) into a short 3₁₀ helix and a dramatically altered Zn-center conformation with no Zn-coordinated. c Overlap of the two full-length rA3G structures based on CD1, which reveals that the CD2 domains in the two structures have different orientations relative to their CD1s. d, e The CD1-CD2 interface interactions of the FKL (D) and E/Q (E) structures. Insets show residues (in sticks) directly participating in CD1-CD2 domain interactions in the two structures respectively (see Supplementary Fig. 4 for list of interacting interface residues in FKL and E/Q structures).