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TitleMechanism of Vps4 hexamer function revealed by cryo-EM.
Journal, issue, pagesSci Adv, Vol. 3, Issue 4, Page e1700325, Year 2017
Publish dateApr 14, 2017
AuthorsMin Su / Emily Z Guo / Xinqiang Ding / Yan Li / Jeffrey T Tarrasch / Charles L Brooks / Zhaohui Xu / Georgios Skiniotis /
PubMed AbstractVps4 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 ...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 conformational changes in a single subunit. The structural transition of the mobile Vps4 subunit results in the repositioning of its substrate-binding loop from the top to the bottom of the central pore, with an associated translation of 33 Å. These structures, along with mutant-doping experiments and functional assays, provide evidence for a sequential and processive ATP hydrolysis mechanism by which Vps4 hexamers disassemble ESCRT-III filaments.
External linksSci Adv / PubMed:28439563 / PubMed Central
MethodsEM (single particle)
Resolution6.0 Å
Structure data

EMDB-8587:
AAA ATPase Vps4 hexamer in closed conformation
Method: EM (single particle) / Resolution: 6.0 Å

EMDB-8588:
AAA ATPase Vps4 hexamer in open conformation
Method: EM (single particle) / Resolution: 6.0 Å

Source
  • Saccharomyces cerevisiae (brewer's yeast)

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