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Comment
. 2022 Feb;32(2):117-118.
doi: 10.1038/s41422-021-00605-7.

SPFH protein cage - one ring to rule them all

Oliver Daumke  1   2 , Gary R Lewin  3
Affiliations
Comment

SPFH protein cage - one ring to rule them all

Oliver Daumke et al. Cell Res. 2022 Feb.
No abstract available

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Figures

Fig. 1
Fig. 1. SPFH protein cages and their substrates.
a Top and bottom views of the HflK/C 24 heteromer, with the N-domain hexamers of four encased FtsH shown in surface representation (magenta). The membrane footprint, indicated by a dashed box, has an approximate area of 16 nm × 16 nm. b Close-up view of the HflK/C heterodimer, showing the domain architecture. The deduced position of the membrane is indicated. c Comparison to other SPFH domain oligomers. Top, the major vault complex (PDB: 4V60) with a 39-fold symmetry. Similar to HFlK/C, the SPFH1, SPFH2 and coiled-coil domains form a cage-like structure with a cap and a shoulder. In the cytosol, two of these oligomers further assemble to build a closed encasing. Bottom, the SPFH2 domains of FliL (PDB: 6AHQ) form a homo-decameric oligomer, using a similar assembly mode to those of HflK/C and the major vault complex. d Schematic illustration showing the rough dimensions of clients of SPFH proteins in the periplasmic/extracellular space (black dashed lines) and at the membrane (red dashed lines). The structures in a, c and d are roughly drawn to scale.
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