5cl2

Publication Abstract from PubMed

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.

Structure of Spo0M, a sporulation-control protein from Bacillus subtilis.,Sonoda Y, Mizutani K, Mikami B Acta Crystallogr F Struct Biol Commun. 2015 Dec 1;71(Pt 12):1488-97. doi:, 10.1107/S2053230X15020919. Epub 2015 Nov 18. PMID:26625291^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.