TY  - JOUR
AU  - Junglas, Benedikt
AU  - Hudina, Esther
AU  - Schönnenbeck, Philipp
AU  - Ritter, Ilona
AU  - Heddier, Anja
AU  - Santiago-Schübel, Beatrix
AU  - Huesgen, Pitter F.
AU  - Schneider, Dirk
AU  - Sachse, Carsten
TI  - Structural plasticity of bacterial ESCRT-III protein PspA in higher-order assemblies
JO  - Nature structural & molecular biology
VL  - 32
SN  - 1545-9993
CY  - London [u.a.]
PB  - Nature Publishing Group
M1  - FZJ-2024-05282
SP  - 23-34
PY  - 2025
AB  - Eukaryotic members of the endosome sorting complex required for transport-III (ESCRT-III) family have been shown to form diverse higher-order assemblies. The bacterial phage shock protein A (PspA) has been identified as a member of the ESCRT-III superfamily, and PspA homo-oligomerizes to form rod-shaped assemblies. As observed for eukaryotic ESCRT-III, PspA forms tubular assemblies of varying diameters. Using electron cryo-electron microscopy, we determined 61 Synechocystis PspA structures and observed in molecular detail how the structural plasticity of PspA rods is mediated by conformational changes at three hinge regions in the monomer and by the fixed and changing molecular contacts between protomers. Moreover, we reduced and increased the structural plasticity of PspA rods by removing the loop connecting helices α3/α4 and the addition of nucleotides, respectively. Based on our analysis of PspA-mediated membrane remodeling, we suggest that the observed mode of structural plasticity is a prerequisite for the biological function of ESCRT-III members.
LB  - PUB:(DE-HGF)16
C6  - 39152237
UR  - <Go to ISI:>//WOS:001292655700003
DO  - DOI:10.1038/s41594-024-01359-7
UR  - https://juser.fz-juelich.de/record/1030409
ER  -