7X59
A Cbc-ParM filament with GTP or GDPPi
Summary for 7X59
| Entry DOI | 10.2210/pdb7x59/pdb |
| EMDB information | 33012 |
| Descriptor | ParM/StbA family protein, GUANOSINE-5'-TRIPHOSPHATE (2 entities in total) |
| Functional Keywords | parm actin-like plasmid segregation, cell cycle |
| Biological source | Clostridium botulinum |
| Total number of polymer chains | 5 |
| Total formula weight | 165342.66 |
| Authors | Koh, A.,Ali, S.,Robinson, R.,Narita, A. (deposition date: 2022-03-04, release date: 2023-03-08, Last modification date: 2025-07-16) |
| Primary citation | Ali, S.,Koh, A.,Popp, D.,Tanaka, K.,Kitaoku, Y.,Miyazaki, N.,Iwasaki, K.,Mitsuoka, K.,Robinson, R.C.,Narita, A. Bacterial genome-encoded ParMs. J.Biol.Chem., 301:110351-110351, 2025 Cited by PubMed Abstract: ParMs generally exist on low-copy number plasmids where they contribute to plasmid segregation and stable inheritance. We carried out bioinformatics analysis, which indicated that ParM genes are not only confined to plasmids but are also occasionally found on genomes. Here we report the discovery and characterization of two chromosome-encoded ParMs (cParMs) from the genomes of Desulfitobacterium hafniense (Dh-cParM1) and Clostridium botulinum (Cb-cParM). Both cParMs form filaments, exhibit nucleotide hydrolysis, and possess characteristic ParM subunit structures. Dh-cParM1 forms single and tightly coupled double filaments and is highly conserved on the chromosomes of five of six Desulfitobacterium species. Interestingly, these bacteria have not been reported to harbor plasmids. Cb-cParM possesses unique properties. Its filaments were stable after nucleotide hydrolysis and Pi release, and its ParR (Cb-cParR) did not affect the initial phase of Cb-cParM polymerization but displayed properties of a depolymerization factor for mature filaments. These results indicate functional, polymerizing ParMs can be encoded on genomes, suggesting that ParM roles may extend to other functions beyond plasmid segregation. PubMed: 40499760DOI: 10.1016/j.jbc.2025.110351 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (6.5 Å) |
Structure validation
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