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. 2017 Jul 17;8:16064. doi: 10.1038/ncomms16064

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Copyright © 2017, The Author(s)

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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(a) Comparison of six pairs of the adjacent Vps4^E233Q subunits. The colouring scheme is the same as in Fig. 1c,e. When one Vps4^E233Q molecule (shown in ribbon representation) from each pair of the adjacent subunits aligned with each other, the other one (shown in cartoon representation) is also well aligned, except for the pairs involving subunit A (red arrow). (b) A focused view of the domains that mediate the interactions between the Vps4^E233Q monomers (subunits C and D). Three boxed intermonomer interfaces are detailed in c–e. (c–e) The close-up views of the interfaces between the large ATPase domains (c), the large and small ATPase domains including the β-domain (d) and the C-terminal helixes (e). Potential residues participated in the interactions are represented by spheres. Hydrophobic, aromatic, positively charged and negatively charged residues are coloured grey, pink, blue and red, respectively. The orientations of all close-up views are optimized to show the interactions. (f–h) SEC analyses of the oligomeric states of the Vps4^E233Q mutants targeting the interface between the large ATPase domains (f), the large and small ATPase domains including the β-domain (g) and the C-terminal helixes (h). (i) A focused view of the interactions between the Vta1 CTD dimer (subunits I and J) and the adjacent Vps4^E233Q subunit pair (subunits C and D). Two different contact modes are highlighted by purple and blue dashed circles, respectively, and detailed in j,k. (j,k) The close-up views of the interactions between the Vps4^E233Q subunit D and the CTD dimer (j), and the Vps4^E233Q subunit C and the CTD dimer (k). (l,m) Assessments of the interactions by SEC between Vta1 and Vps4 mutants, E233Q and E233QR325A, at high concentration (100 μM) in the absence of ATP (l), and at low concentration (5 μM) in the presence of ATP (m). (n) Assessment of the stabilities of the Vta1-free Vps4^E233Q hexamer and the Vta1-bound Vps4^E233Q hexamer formed by different Vps4 mutants with or without apyrase treatment by SEC (See Methods for details).