Crystallization and preliminary X-ray diffraction studies of HutP protein: an RNA-binding protein that regulates the transcription of hut operon in Bacillus subtilis.
HutP is an RNA-binding protein and regulates the expression of the histidine utilization (hut) operon in Bacillus subtilis by binding to cis-acting regulatory sequences on hut mRNA. HutP and its mutant, which has increased affinity for the regulatory sequences, were purified and crystallized by the hanging-drop vapor diffusion method. The space group was P2(1)3 with unit cell dimensions a=b=c=95.6A for HutP and a=b=c=96.8A for the mutant. Complete data sets of 3.0-A resolution for wild-type HutP and of 2.70-A resolution for the mutant HutP were collected.
Kumarevel
T S
TS
Institute of Molecular and Cell Biology, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba Central 6, Tsukuba, Ibaraki 305-8566, Japan.
Fujimoto
Z
Z
Padmanabhan
B
B
Oda
M
M
Nishikawa
S
S
Mizuno
H
H
Kumar
P K R
PK
D001412:Bacillus subtilis / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D009876:Operon; D016601:RNA-Binding Proteins / Q000737:chemistry*; D014961:X-Ray Diffraction / Q000379:methods*
D001426:Bacterial Proteins; D016601:RNA-Binding Proteins