Figure 4. Vta1^VSL contacts with Vps4.

(A) Density for the most clearly defined Vta1^VSL (bound to the Vps4 subunit A β domain). The Vta1^VSL subunits are colored tan and teal. (B) Vta1^VSL interaction with the first Vps4 subunit. This interface is modeled identically to a crystal structure of Vta1^VSL in complex with a truncated Vps4 construct (Yang and Hurley, 2010). Additional N-terminal residues in the longer Vta1 construct used in this study are shown in white and their interaction with the small AAA ATPase domain of Vps4 is indicated with an asterisk. (C) Vta1^VSL interaction with the second Vps4 subunit. Y303’ and Y310’ are labeled. (D) Overlap of subunit pairs on the small AAA ATPase domain of the first Vps4 (residues 301–349 and 403–411). Consequent RMSD values are shown for residues 300–311 and 320–331 of the second Vps4 subunit at the second Vta1 interface (asterisk).

DOI: http://dx.doi.org/10.7554/eLife.24487.018

Figure 4—figure supplement 1. Rigid-body fitting of Vps4 β domain-Vta1^VSL complexes into each density map.

(A) The A-B, B-C, C-D, and F-A Vta1^VSL dimers show density for distinct helices. Density for D-E and E-F Vta1^VSL dimers is poor and only S and β domain coordinates were used for rigid body fitting at these two interfaces. (B) Side view of the fitting at the A-B interface as in panel (A) showing distinct density for each of the four Vta1^VSL helices. (C) Low threshold view of the A-B map reveals extensions of the Vta1^VSL density that can accommodate the additional N-terminal residues included in our Vta1 construct (black ribbon).

DOI: http://dx.doi.org/10.7554/eLife.24487.019