%0 Journal Article
%A Hudina, Esther
%A Junglas, Benedikt
%A Sachse, Carsten
%T Plastizität bakterieller ESCRT-III-Strukturen bei der Membranremodellierung
%J Biospektrum
%V 31
%N 7
%@ 0947-0867
%C Heidelberg
%I Springer Nature
%M FZJ-2025-05180
%P 723 - 726
%D 2025
%X 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.
%F PUB:(DE-HGF)16
%9 Journal Article
%R 10.1007/s12268-025-2597-3
%U https://juser.fz-juelich.de/record/1049088