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Title: Cryo-EM structure of the entire FtsH-HflKC AAA protease complex
Authors: Qiao, Zhu
Yokoyama, Tatsuhiko
Yan, Xin-Fu
Beh, Ing Tsyr
Shi, Jian
Basak, Sandip
Akiyama, Yoshinori
Gao, Yong-Gui
Keywords: Science::Biological sciences
Issue Date: 2022
Source: Qiao, Z., Yokoyama, T., Yan, X., Beh, I. T., Shi, J., Basak, S., Akiyama, Y. & Gao, Y. (2022). Cryo-EM structure of the entire FtsH-HflKC AAA protease complex. Cell Reports, 39(9), 110890-.
Project: MOE2019-T2-2-099
Journal: Cell Reports
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.
ISSN: 2211-1247
DOI: 10.1016/j.celrep.2022.110890
Schools: School of Biological Sciences 
Research Centres: NTU Institute of Structural Biology 
Rights: © 2022 The Author(s). This is an open access article under the CC BY-NC-ND license (
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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