Expression, purification, crystallization and preliminary X-ray analysis of two arginine-biosynthetic enzymes from Mycobacterium tuberculosis.
The gene products of two open reading frames from Mycobacterium tuberculosis (Mtb) have been crystallized using the sitting-drop vapour-diffusion method. Rv1652 encodes a putative N-acetyl-gamma-glutamyl-phosphate reductase (MtbAGPR), while the Rv1656 gene product is annotated as ornithine carbamoyltransferase (MtbOTC). Both MtbAGPR and MtbOTC were expressed in Escherichia coli, purified to homogeneity and crystallized. Native data for each crystal were collected to resolutions of 2.15 and 2.80 A, respectively. Preliminary X-ray data are presented for both enzymes.
Moradian
Fatemeh
F
Protein Structure and Function Group, Department of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2H7, Canada.
Garen
Craig
C
Cherney
Leonid
L
Cherney
Maia
M
James
Michael N G
MN
D000445:Aldehyde Oxidoreductases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D001120:Arginine / Q000096:biosynthesis*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D009169:Mycobacterium tuberculosis / Q000201:enzymology*; D009954:Ornithine Carbamoyltransferase / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification
D001426:Bacterial Proteins; D001120:Arginine; D000445:Aldehyde Oxidoreductases; C018722:N-acetyl-gamma-glutamyl-phosphate reductase; D009954:Ornithine Carbamoyltransferase