6OO2

Vps4 with Cyclic Peptide Bound in the Central Pore

6OO2 の概要

• エントリーDOI: 10.2210/pdb6oo2/pdb
• EMDBエントリー: 20139 20140 20141 20142 20144 20147
• 分子名称: Vacuolar protein sorting-associated protein 4, Designed Cyclic Peptide, Vacuolar protein sorting-associated protein VTA1, ... (6 entities in total)
• 機能のキーワード: vps4, escrt, vta1, aaa atpase, transport protein
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 19
• 化学式量合計: 297099.57

構造登録者

Han, H.,Fulcher, J.M.,Dandey, V.P.,Sundquist, W.I.,Kay, M.S.,Shen, P.,Hill, C.P. (登録日: 2019-04-22, 公開日: 2019-08-21, 最終更新日: 2024-03-20)

主引用文献

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

実験手法

ELECTRON MICROSCOPY (4.4 Å)