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Structure of Spo0M, a sporulation‐control protein from Bacillus subtilis
Author(s) -
Sonoda Yo,
Mizutani Kimihiko,
Mikami Bunzo
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x15020919
Subject(s) - bacillus subtilis , structural similarity , protein structure , homology (biology) , crystal structure , peptide sequence , protein domain , biology , amino acid , arrestin , protein data bank (rcsb pdb) , c terminus , crystallography , biochemistry , chemistry , genetics , gene , receptor , bacteria , g protein coupled receptor
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.