5CL2: Crystal Structure Of Spo0m, Sporulation Control Protein, From Bacillus Subtilis

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 A. 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 beta-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.
PDB ID: 5CL2Download
MMDB ID: 134858
PDB Deposition Date: 2015/7/16
Updated in MMDB: 2015/12
Experimental Method:
x-ray diffraction
Resolution: 2.3  Å
Source Organism:
Similar Structures:
Biological Unit for 5CL2: dimeric; determined by author
Molecular Components in 5CL2
Label Count Molecule
Proteins (2 molecules)
Sporulation-control Protein Spo0m(Gene symbol: spo0M)
Molecule annotation
Chemicals (2 molecules)
* Click molecule labels to explore molecular sequence information.

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