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Comment
. 2024 Aug 20;121(34):e2413203121.
doi: 10.1073/pnas.2413203121. Epub 2024 Aug 12.

Revealing the architecture of the membrane-bound Flotillin cage assembly

Brett M Collins  1
Affiliations
Comment

Revealing the architecture of the membrane-bound Flotillin cage assembly

Brett M Collins. Proc Natl Acad Sci U S A. .
No abstract available

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Conflict of interest statement

Competing interests statement:The author declares no competing interest.

Figures

Fig. 1.
Fig. 1.
Flotillin structure and comparison to other SPFH assemblies. (A) Domain organization of the human Flotillin-1 and Flotillin-2 proteins. (B) Structure of the Flotillin-1/Flotillin-2 cage determined by single-particle cryoEM (PDB ID: 9BQ2) (11). The cage is composed of 44 monomers with 22 copies of each protein (Flotillin-1 in blue and Flotillin-2 in yellow). The N-terminal SPFH1 domain forms the wider base of the structure embedded within the lipid bilayer by aromatic residues and lipid-modified sidechains. (C) The walls of the cage are formed by the extended α-helical domains (CC1) that interact with each other through alternating charged sidechains. Examples are shown of the inside (Left) and outside (Right) of the cage. (D) The bacterial HflK/HflC proteins (cyan and light purple) form a similar cage but with a different stoichiometry and including N-terminal transmembrane (TM) domains (PDB ID: 7WI3) (10). The HflK/HflC complex is also able to cluster and compartmentalize four copies of the FtsH AAA ATPase (shown in purple surface representation). The Vault assembly formed by the major Vault protein has a similar organization but includes multiple copies of the SPFH1 module and forms a closed capsid (PDB ID: 4V60) (12). Images were made with ChimeraX (13).
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References

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