5CL2
Crystal structure of Spo0M, sporulation control protein, from Bacillus subtilis.
Summary for 5CL2
| Entry DOI | 10.2210/pdb5cl2/pdb |
| Descriptor | Sporulation-control protein spo0M, SODIUM ION (3 entities in total) |
| Functional Keywords | sporulation, spo0m, protein binding |
| Biological source | Bacillus subtilis (strain 168) |
| Total number of polymer chains | 2 |
| Total formula weight | 58174.73 |
| Authors | Sonoda, Y.,Mizutani, K.,Mikami, B. (deposition date: 2015-07-16, release date: 2015-12-16, Last modification date: 2024-03-20) |
| Primary citation | Sonoda, Y.,Mizutani, K.,Mikami, B. Structure of Spo0M, a sporulation-control protein from Bacillus subtilis. Acta Crystallogr.,Sect.F, 71:1488-1497, 2015 Cited by PubMed Abstract: Spo0M is a sporulation-control protein that is thought to play an essential role in the early stage of endospore formation. While little is known about the functions of Spo0M, a recent phylogenetic study suggests that, based on its amino-acid sequence, Spo0M might belong to the arrestin clan. The crystal structure of the Spo0M protein was determined at a resolution of 2.3 Å. Ten amino acids at the end of the N-terminus were removed to improve the thermal stability of the purified Spo0M protein and the crystal structure of Spo0M was determined by SAD. Spo0M has a well conserved N-terminal domain with an arrestin-like fold, which consists of a β-strand sandwich structure. Surprisingly, the C-terminal domain of Spo0M, which has no structural homology to arrestin-clan proteins, bears significant structural similarity to the FP domain of the human PI31 protein. In addition, Spo0M harbours a potential polar-core structure connecting the N- and C-terminal domains with several salt bridges, as seen in the crystal structures of arrestin and VPS26. The structure reported here constitutes the first structural information on a bacterial protein that shares significant structural homology to members of the arrestin clan and the FP domain. PubMed: 26625291DOI: 10.1107/S2053230X15020919 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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