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-Structure paper
タイトル | Molecular basis for curvature formation in SepF polymerization. |
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ジャーナル・号・ページ | Proc Natl Acad Sci U S A, Vol. 121, Issue 9, Page e2316922121, Year 2024 |
掲載日 | 2024年2月27日 |
著者 | Wenjing Liu / Chang Zhang / Huawei Zhang / Shaojie Ma / Jing Deng / Daping Wang / Ziwei Chang / Jun Yang / |
PubMed 要旨 | 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 ...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. |
リンク | Proc Natl Acad Sci U S A / PubMed:38381790 / PubMed Central |
手法 | EM (単粒子) / NMR (固体) |
解像度 | 7.32 Å |
構造データ | EMDB-35112: Cryo-EM map of SepF PDB-8hzq: PDB-8hzt: |
由来 |
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キーワード | PROTEIN FIBRIL / Cell division / Assembly / Interact with Z-ring / membrane-binding protein / Fibril assembly / Single point mutation |