8HZT
Bacillus subtilis SepF protein assembly (G137N mutant)
Summary for 8HZT
| Entry DOI | 10.2210/pdb8hzt/pdb |
| Descriptor | Cell division protein SepF (1 entity in total) |
| Functional Keywords | cell division, fibril assembly, single point mutation, protein fibril |
| Biological source | Bacillus subtilis |
| Total number of polymer chains | 2 |
| Total formula weight | 17810.16 |
| Authors | |
| Primary citation | 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 Cited by 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: 38381790DOI: 10.1073/pnas.2316922121 PDB entries with the same primary citation |
| Experimental method | SOLID-STATE NMR |
Structure validation
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