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-Structure paper
タイトル | Cryo-EM structure of the entire FtsH-HflKC AAA protease complex. |
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ジャーナル・号・ページ | Cell Rep, Vol. 39, Issue 9, Page 110890, Year 2022 |
掲載日 | 2022年5月31日 |
著者 | Zhu Qiao / Tatsuhiko Yokoyama / Xin-Fu Yan / Ing Tsyr Beh / Jian Shi / Sandip Basak / Yoshinori Akiyama / Yong-Gui Gao / |
PubMed 要旨 | 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 ...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. |
リンク | Cell Rep / PubMed:35649372 |
手法 | EM (単粒子) |
解像度 | 3.4 - 6.8 Å |
構造データ | EMDB-32520: Cryo-EM structure of E.coli membrane protein complex EMDB-32521: Cryo-EM structure of E.coli membrane protein complex EMDB-32522: Cryo-EM map of the entire FtsH-HflKC AAA protease EMDB-32523: Cryo-EM map of FtsH periplasmic domain and transmembrane helices EMDB-32524: Cryo-EM map of E.coli FtsH AAA protease |
化合物 | ChemComp-ANP: ChemComp-ZN: ChemComp-MG: |
由来 |
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キーワード | MEMBRANE PROTEIN / complex / HYDROLASE |