Crystallization and preliminary X-ray studies of SdiA from Escherichia coli.
SdiA enhances cell division by regulating the ftsQAZ operon in Escherichia coli as a transcription activator. In addition, SdiA is suggested to play a role in detecting quorum signals that emanate from other species. It is therefore a homologue of LuxR, a cognate quorum-sensing receptor that recognizes a quorum signal and activates the quorum responses. To elucidate the role of SdiA and its functional and structural relationship to LuxR, structural studies were performed on E. coli SdiA. Recombinant SdiA was overexpressed, purified and crystallized at 287 K using the hanging-drop vapour-diffusion method. X-ray diffraction data from a native crystal were collected with 99.7% completeness to 2.7 A resolution with an R(merge) of 6.0%. The crystals belong to the hexagonal space group P6(1)22 or P6(5)22, with unit-cell parameters a = b = 130.47, c = 125.23 A.
Wu
Chunai
C
Department of Molecular Cell Biology, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon 440-746, Republic of Korea.
Lokanath
Neratur K
NK
Kim
Dong Young
DY
Nguyen
Lan Dao Ngoc
LD
Kim
Kyeong Kyu
KK
D003227:Conjugation, Genetic; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D010957:Plasmids; D011994:Recombinant Proteins / Q000737:chemistry; D015534:Trans-Activators / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D014961:X-Ray Diffraction
D029968:Escherichia coli Proteins; D011994:Recombinant Proteins; D015534:Trans-Activators; C490806:sdiA protein, E coli