6NDY

Vps4 with Cyclic Peptide Bound in the Central Pore

Summary for 6NDY

• Entry DOI: 10.2210/pdb6ndy/pdb
• EMDB information: 0443
• Descriptor: Vacuolar protein sorting-associated protein 4, Designed Cyclic Peptide, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• Functional Keywords: vps4, escrt, vta1, aaa atpase, transport protein, transport protein-peptide complex, transport protein/peptide
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Total number of polymer chains: 6
• Total formula weight: 190695.04

Authors

Han, H.,Fulcher, J.M.,Dandey, V.P.,Sundquist, W.I.,Kay, M.S.,Shen, P.,Hill, C.P. (deposition date: 2018-12-14, release date: 2019-08-21, Last modification date: 2024-03-20)

Primary citation

Han, H.,Fulcher, J.M.,Dandey, V.P.,Iwasa, J.H.,Sundquist, W.I.,Kay, M.S.,Shen, P.S.,Hill, C.P.
Structure of Vps4 with circular peptides and implications for translocation of two polypeptide chains by AAA+ ATPases.
Elife, 8:-, 2019

PubMed Abstract: Many AAA+ ATPases form hexamers that unfold protein substrates by translocating them through their central pore. Multiple structures have shown how a helical assembly of subunits binds a single strand of substrate, and indicate that translocation results from the ATP-driven movement of subunits from one end of the helical assembly to the other end. To understand how more complex substrates are bound and translocated, we demonstrated that linear and cyclic versions of peptides bind to the AAA+ ATPase Vps4 with similar affinities, and determined cryo-EM structures of cyclic peptide complexes. The peptides bind in a hairpin conformation, with one primary strand equivalent to the single chain peptide ligands, while the second strand returns through the translocation pore without making intimate contacts with Vps4. These observations indicate a general mechanism by which AAA+ ATPases may translocate a variety of substrates that include extended chains, hairpins, and crosslinked polypeptide chains.

PubMed: 31184588
DOI: 10.7554/eLife.44071

Experimental method

ELECTRON MICROSCOPY (3.6 Å)