5CL2

Crystal structure of Spo0M, sporulation control protein, from Bacillus subtilis.

5CL2 の概要

• エントリーDOI: 10.2210/pdb5cl2/pdb
• 分子名称: Sporulation-control protein spo0M, SODIUM ION (3 entities in total)
• 機能のキーワード: sporulation, spo0m, protein binding
• 由来する生物種: Bacillus subtilis (strain 168)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 58174.73

構造登録者

Sonoda, Y.,Mizutani, K.,Mikami, B. (登録日: 2015-07-16, 公開日: 2015-12-16, 最終更新日: 2024-03-20)

主引用文献

Sonoda, Y.,Mizutani, K.,Mikami, B.
Structure of Spo0M, a sporulation-control protein from Bacillus subtilis.
Acta Crystallogr.,Sect.F, 71:1488-1497, 2015

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: 26625291
DOI: 10.1107/S2053230X15020919

実験手法

X-RAY DIFFRACTION (2.3 Å)