TY  - JOUR
AU  - Hudina, Esther
AU  - Junglas, Benedikt
AU  - Sachse, Carsten
TI  - Plastizität bakterieller ESCRT-III-Strukturen bei der Membranremodellierung
JO  - Biospektrum
VL  - 31
IS  - 7
SN  - 0947-0867
CY  - Heidelberg
PB  - Springer Nature
M1  - FZJ-2025-05180
SP  - 723 - 726
PY  - 2025
AB  - Bacterial ESCRT-III proteins protect and maintain the structural integrity of prokaryotic membranes. Cryo-electron microscopy studies of ESCRT-III family members PspA and Vipp1 revealed the structural basis of helical rod, ring and stacked ring assembly formation. Although the basic ESCRT-III fold remained conserved in the observed structures, monomers adopted a remarkable degree of structural plasticity. Minor conformational changes resulted in major shifts in assembly architectures and are important for the ability to remodel membranes.
LB  - PUB:(DE-HGF)16
DO  - DOI:10.1007/s12268-025-2597-3
UR  - https://juser.fz-juelich.de/record/1049088
ER  -