Journal Article

FZJ-2025-05180

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Plastizität bakterieller ESCRT-III-Strukturen bei der Membranremodellierung

Hudina, E.FZJ* ; Junglas, B.FZJ* ; Sachse, C. (Corresponding author)FZJ*

2025
Springer Nature Heidelberg

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Please use a persistent id in citations: doi:10.1007/s12268-025-2597-3  doi:10.34734/FZJ-2025-05180

Abstract: 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.

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Contributing Institute(s):

1. Strukturbiologie (ER-C-3)

Research Program(s):

1. 5352 - Understanding the Functionality of Soft Matter and Biomolecular Systems (POF4-535) (POF4-535)
2. 5241 - Molecular Information Processing in Cellular Systems (POF4-524) (POF4-524)

Appears in the scientific report 2025

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Database coverage:
; ; DEAL Springer ; SCOPUS

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