Crystallization and preliminary X-ray crystallographic studies of DesR, a thermosensing response regulator in a two-component signalling system from Streptococcus pneumoniae.
The response regulator DesR, which activates the transcription of the des gene by binding to a regulatory region, is essential for controlling the fluidity of membrane phospholipids. DesR from Streptococcus pneumoniae was overexpressed in Escherichia coli. The protein was purified and crystallized for structural analysis. Diffraction data were collected to 1.7 A resolution using synchrotron radiation and the crystals belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 46.91, b = 71.38, c = 117.73 A. Assuming the presence of a dimer in the asymmetric unit, this corresponds to a V(M) of 2.21 A(3) Da(-1).
Park
Ae Kyung
AK
Division of Biotechnology, College of Life Sciences, Korea University, Seoul 136-713, Republic of Korea.
Bong
Seung Min
SM
Moon
Jin Ho
JH
Chi
Young Min
YM
D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D015398:Signal Transduction; D013296:Streptococcus pneumoniae / Q000737:chemistry*; D013696:Temperature
D001426:Bacterial Proteins