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. 2017 Nov 2;7:14893. doi: 10.1038/s41598-017-14194-2

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© The Author(s) 2017

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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Comparison of katanin p60-MIT interactions with those of other AAA+ ATPses. (A–E) The structures of different MIT domains are highly similar to each other and they all form an asymmetric three-helix bundle. Superimposition of available complex structures demonstrates an overlap of the binding motifs, although the molecular contacts between these complexes are in most cases not conserved. (A) Spastin-CHMP1B structure (PDB ID 3EAB), (B) ATG1-ATG13 structure (PDB ID 4P1N), (C) Vps4-Vps2 structure (PDB ID 2V6X), (D) Vps4-CHMP6 structure (PDB ID 2K3W), (E) VPS4-Vfa1 structure (PDB ID 5FVK).