Expression, crystallization and preliminary crystallographic analysis of the PAS domain of RsbP, a stress-response phosphatase from Bacillus subtilis.
RsbP, a regulator of RNA polymerase sigma(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-sigma(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 P2(1), with unit-cell parameters a = 55.2, b = 71.7, c = 60.2 A, beta = 92.1 degrees . Diffraction data were collected to a resolution of 1.6 A.
Makino
Masatomo
M
Japan Synchrotron Radiation Research Institute/SPring-8, Japan.
Kondo
Shinpei
S
Kaneko
Tomonori
T
Baba
Seiki
S
Hirata
Kunio
K
Kumasaka
Takashi
T
D001412:Bacillus subtilis / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D003625:Data Collection; D005798:Genes, Bacterial; D010750:Phosphoproteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D010744:Phosphoric Monoester Hydrolases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D013223:Statistics as Topic; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D010750:Phosphoproteins; D011994:Recombinant Proteins; C119218:RsbR protein, Bacillus subtilis; D010744:Phosphoric Monoester Hydrolases