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Structure paper

TitleCryo-EM structure of the entire FtsH-HflKC AAA protease complex.
Journal, issue, pagesCell Rep, Vol. 39, Issue 9, Page 110890, Year 2022
Publish dateMay 31, 2022
AuthorsZhu Qiao / Tatsuhiko Yokoyama / Xin-Fu Yan / Ing Tsyr Beh / Jian Shi / Sandip Basak / Yoshinori Akiyama / Yong-Gui Gao /
PubMed AbstractThe 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.
External linksCell Rep / PubMed:35649372
MethodsEM (single particle)
Resolution3.4 - 6.8 Å
Structure data

32520

7wi3

EMDB-32520, PDB-7wi3:
Cryo-EM structure of E.Coli FtsH-HflkC AAA protease complex
Method: EM (single particle) / Resolution: 4.0 Å

32521

7wi4

EMDB-32521, PDB-7wi4:
Cryo-EM structure of E.Coli FtsH protease cytosolic domains
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-32522: Cryo-EM map of the entire FtsH-HflKC AAA protease
Method: EM (single particle) / Resolution: 6.8 Å

EMDB-32523: Cryo-EM map of FtsH periplasmic domain and transmembrane helices
Method: EM (single particle) / Resolution: 6.5 Å

EMDB-32524: Cryo-EM map of E.coli FtsH AAA protease
Method: EM (single particle) / Resolution: 4.2 Å

Chemicals

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

ChemComp-ZN:
Unknown entry

ChemComp-MG:
Unknown entry

Source
  • Escherichia coli (strain K12) (bacteria)
  • escherichia coli k-12 (bacteria)
  • Escherichia coli (E. coli)
KeywordsMEMBRANE PROTEIN / complex / HYDROLASE

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