7E1C
Structure of MreB3 from Spiroplasma eriocheiris
Summary for 7E1C
| Entry DOI | 10.2210/pdb7e1c/pdb |
| Descriptor | Cell shape-determining protein MreB, ACETATE ION, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | cytoskeleton, actin homolog, structural protein |
| Biological source | Spiroplasma eriocheiris |
| Total number of polymer chains | 1 |
| Total formula weight | 39051.60 |
| Authors | Takahashi, D.,Miyata, M.,Imada, K. (deposition date: 2021-02-01, release date: 2022-02-16, Last modification date: 2023-11-29) |
| Primary citation | Takahashi, D.,Fujiwara, I.,Sasajima, Y.,Narita, A.,Imada, K.,Miyata, M. ATP-dependent polymerization dynamics of bacterial actin proteins involved in Spiroplasma swimming. Open Biology, 12:220083-220083, 2022 Cited by PubMed Abstract: MreB is a bacterial protein belonging to the actin superfamily. This protein polymerizes into an antiparallel double-stranded filament that determines cell shape by maintaining cell wall synthesis. , a helical wall-less bacterium, has five MreB homologous (SpeMreB1-5) that probably contribute to swimming motility. Here, we investigated the structure, ATPase activity and polymerization dynamics of SpeMreB3 and SpeMreB5. SpeMreB3 polymerized into a double-stranded filament with possible antiparallel polarity, while SpeMreB5 formed sheets which contained the antiparallel filament, upon nucleotide binding. SpeMreB3 showed slow P release owing to the lack of an amino acid motif conserved in the catalytic centre of MreB family proteins. Our SpeMreB3 crystal structures and analyses of SpeMreB3 and SpeMreB5 variants showed that the amino acid motif probably plays a role in eliminating a nucleophilic water proton during ATP hydrolysis. Sedimentation assays suggest that SpeMreB3 has a lower polymerization activity than SpeMreB5, though their polymerization dynamics are qualitatively similar to those of other actin superfamily proteins, in which pre-ATP hydrolysis and post-P release states are unfavourable for them to remain as filaments. PubMed: 36285441DOI: 10.1098/rsob.220083 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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