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<p>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.</p>

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Plastizität bakterieller ESCRT-III-Strukturen bei der Membranremodellierung

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年11月22日

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  • Esther Hudina,
  • Benedikt Junglas,
  • Carsten Sachse

摘要

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.