8HZT

Bacillus subtilis SepF protein assembly (G137N mutant)

8HZT の概要

• エントリーDOI: 10.2210/pdb8hzt/pdb
• 分子名称: Cell division protein SepF (1 entity in total)
• 機能のキーワード: cell division, fibril assembly, single point mutation, protein fibril
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 17810.16

構造登録者

Liu, W. (登録日: 2023-01-09, 公開日: 2024-02-14, 最終更新日: 2024-05-15)

主引用文献

Liu, W.,Zhang, C.,Zhang, H.,Ma, S.,Deng, J.,Wang, D.,Chang, Z.,Yang, J.
Molecular basis for curvature formation in SepF polymerization.
Proc.Natl.Acad.Sci.USA, 121:e2316922121-e2316922121, 2024

PubMed Abstract: The self-assembly of proteins into curved structures plays an important role in many cellular processes. One good example of this phenomenon is observed in the septum-forming protein (SepF), which forms polymerized structures with uniform curvatures. SepF is essential for regulating the thickness of the septum during bacteria cell division. In , SepF polymerization involves two distinct interfaces, the β-β and α-α interfaces, which define the assembly unit and contact interfaces, respectively. However, the mechanism of curvature formation in this step is not yet fully understood. In this study, we employed solid-state NMR (SSNMR) to compare the structures of cyclic wild-type SepF assemblies with linear assemblies resulting from a mutation of G137 on the β-β interface. Our results demonstrate that while the sequence differences arise from the internal assembly unit, the dramatic changes in the shape of the assemblies depend on the α-α interface between the units. We further provide atomic-level insights into how the angular variation of the α2 helix on the α-α interface affects the curvature of the assemblies, using a combination of SSNMR, cryo-electron microscopy, and simulation methods. Our findings shed light on the shape control of protein assemblies and emphasize the importance of interhelical contacts in retaining curvature.

PubMed: 38381790
DOI: 10.1073/pnas.2316922121

実験手法

SOLID-STATE NMR