Open AccessExpression, crystallization and preliminary crystallographic analysis of the PAS domain of RsbP, a stress‐response phosphatase from Bacillus subtilis
Author(s) -
Makino Masatomo,
Kondo Shinpei,
Kaneko Tomonori,
Baba Seiki,
Hirata Kunio,
Kumasaka Takashi
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109014158
Subject(s) - bacillus subtilis , crystallization , crystallography , phosphatase , domain (mathematical analysis) , stress (linguistics) , materials science , expression (computer science) , biophysics , chemistry , biochemistry , biology , enzyme , genetics , computer science , mathematics , bacteria , organic chemistry , mathematical analysis , linguistics , philosophy , programming language
RsbP, a regulator of RNA polymerase σ B activity in Bacillus subtilis , is a phosphatase containing a Per–Arnt–Sim (PAS) domain in its N‐terminal region that is expected to sense energy stresses such as carbon, phosphate or oxygen starvation. Energy‐stress signals are transmitted to the PAS domain and activate the C‐terminal phosphatase domain of RsbP, leading to activation of the downstream anti‐anti‐σ B factor RsbV. Finally, the general stress response is induced to protect the cells against further stresses. The recombinant PAS domain of RsbP was crystallized by the sitting‐drop vapour‐diffusion technique using 40% PEG 400 as a precipitant. The crystals belonged to space group P 2 1 , with unit‐cell parameters a = 55.2, b = 71.7, c = 60.2 Å, β = 92.1°. Diffraction data were collected to a resolution of 1.6 Å.