Expression, purification and preliminary X-ray analysis of the C-terminal domain of an arginine repressor protein from Mycobacterium tuberculosis.
The gene product of an open reading frame Rv1657 from Mycobacterium tuberculosis is a putative arginine repressor protein (ArgR), a transcriptional factor that regulates the expression of arginine-biosynthetic enzymes. Rv1657 was expressed and purified and a C-terminal domain was crystallized using the hanging-drop vapour-diffusion method. Diffraction data were collected and processed to a resolution of 2.15 A. The crystals belong to space group P1 and the Matthews coefficient suggests that the crystals contain six C-terminal domain molecules per unit cell. Previous structural and biochemical studies on the arginine repressor proteins from other organisms have likewise shown the presence of six molecules per unit cell.
Lu
George J
GJ
Protein Structure and Function Group, Department of Biochemistry, The University of Alberta, Edmonton, Alberta T6G 2H7, Canada.
Garen
Craig R
CR
Cherney
Maia M
MM
Cherney
Leonid T
LT
Lee
Cecilia
C
James
Michael N G
MN
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D009169:Mycobacterium tuberculosis / Q000737:chemistry; D012097:Repressor Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification; D016415:Sequence Alignment
C087018:ArgR protein, Bacteria; D001426:Bacterial Proteins; D012097:Repressor Proteins