7WI4

Cryo-EM structure of E.Coli FtsH protease cytosolic domains

7WI4 の概要

• エントリーDOI: 10.2210/pdb7wi4/pdb
• EMDBエントリー: 32521
• 分子名称: ATP-dependent zinc metalloprotease FtsH, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ZINC ION, ... (4 entities in total)
• 機能のキーワード: complex, membrane protein, hydrolase
• 由来する生物種: Escherichia coli K-12
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 428345.79

構造登録者

Qiao, Z.,Gao, Y.G. (登録日: 2022-01-02, 公開日: 2022-06-01, 最終更新日: 2024-06-26)

主引用文献

Qiao, Z.,Yokoyama, T.,Yan, X.F.,Beh, I.T.,Shi, J.,Basak, S.,Akiyama, Y.,Gao, Y.G.
Cryo-EM structure of the entire FtsH-HflKC AAA protease complex.
Cell Rep, 39:110890-110890, 2022

PubMed Abstract: The membrane-bound AAA protease FtsH is the key player controlling protein quality in bacteria. Two single-pass membrane proteins, HflK and HflC, interact with FtsH to modulate its proteolytic activity. Here, we present structure of the entire FtsH-HflKC complex, comprising 12 copies of both HflK and HflC, all of which interact reciprocally to form a cage, as well as four FtsH hexamers with periplasmic domains and transmembrane helices enclosed inside the cage and cytoplasmic domains situated at the base of the cage. FtsH K61/D62/S63 in the β2-β3 loop in the periplasmic domain directly interact with HflK, contributing to complex formation. Pull-down and in vivo enzymatic activity assays validate the importance of the interacting interface for FtsH-HflKC complex formation. Structural comparison with the substrate-bound human m-AAA protease AFG3L2 offers implications for the HflKC cage in modulating substrate access to FtsH. Together, our findings provide a better understanding of FtsH-type AAA protease holoenzyme assembly and regulation.

PubMed: 35649372
DOI: 10.1016/j.celrep.2022.110890

実験手法

ELECTRON MICROSCOPY (3.4 Å)