Mechanism of Vps4 hexamer function revealed by cryo-EM.

ABSTRACT: Vps4 is a member of AAA⁺ ATPase (adenosine triphosphatase associated with diverse cellular activities) that operates as an oligomer to disassemble ESCRT-III (endosomal sorting complex required for transport III) filaments, thereby catalyzing the final step in multiple ESCRT-dependent membrane remodeling events. We used electron cryo-microscopy to visualize oligomers of a hydrolysis-deficient Vps4 (vacuolar protein sorting-associated protein 4) mutant in the presence of adenosine 5'-triphosphate (ATP). We show that Vps4 subunits assemble into an asymmetric hexameric ring following an approximate helical path that sequentially stacks substrate-binding loops along the central pore. The hexamer is observed to adopt an open or closed ring configuration facilitated by major conformati

SUBMITTER: Su M 

PROVIDER: S-EPMC5392032 | biostudies-literature | 2017 Apr

REPOSITORIES: biostudies-literature