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TitleStructure of Vps4 with circular peptides and implications for translocation of two polypeptide chains by AAA+ ATPases.
Journal, issue, pagesElife, Vol. 8, Year 2019
Publish dateJun 11, 2019
AuthorsHan Han / James M Fulcher / Venkata P Dandey / Janet H Iwasa / Wesley I Sundquist / Michael S Kay / Peter S Shen / Christopher P Hill /
PubMed AbstractMany 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 ...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.
External linksElife / PubMed:31184588 / PubMed Central
MethodsEM (single particle)
Resolution3.6 - 4.4 Å
Structure data

0443

6ndy

EMDB-0443, PDB-6ndy:
Vps4 with Cyclic Peptide Bound in the Central Pore
Method: EM (single particle) / Resolution: 3.6 Å

EMDB-20139:
Vps4 with Cyclic Peptide Bound in the Central Pore (Focused Classification of Subunit F, State1)
Method: EM (single particle) / Resolution: 3.9 Å

EMDB-20140:
Vps4 with Cyclic Peptide Bound in the Central Pore (Focused Classification of Subunit F, State2)
Method: EM (single particle) / Resolution: 3.8 Å

EMDB-20141:
Vps4 with Cyclic Peptide Bound in the Central Pore (Focused Classification of Subunit F, State3)
Method: EM (single particle) / Resolution: 4.3 Å

20142

6oo2

EMDB-20142, PDB-6oo2:
Vps4 with Cyclic Peptide Bound in the Central Pore
Method: EM (single particle) / Resolution: 4.4 Å

EMDB-20144:
Vps4 with Cyclic Peptide Bound in the Central Pore (Map for Peptide cF30)
Method: EM (single particle) / Resolution: 3.8 Å

EMDB-20147:
Vps4 with Cyclic Peptide Bound in the Central Pore (Map for Peptide cFF30)
Method: EM (single particle) / Resolution: 4.0 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

ChemComp-BEF:
BERYLLIUM TRIFLUORIDE ION

ChemComp-MG:
Unknown entry

Source
  • saccharomyces cerevisiae (brewer's yeast)
  • synthetic construct (others)
KeywordsTRANSPORT PROTEIN/PEPTIDE / Vps4 / ESCRT / Vta1 / AAA ATPase / TRANSPORT PROTEIN / TRANSPORT PROTEIN-PEPTIDE complex

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