Crystallization and preliminary crystallographic analysis of N-acetyltransferase Mpr1 from Saccharomyces cerevisiae.
Mpr1 is an enzyme that catalyzes the N-acetylation of the toxic L-azetidine-2-carboxylic acid (AZC). Recently, Mpr1 has been shown to reduce levels of intracellular reactive oxygen species (ROS) under oxidative stress. The natural substrate involved in the ROS elimination in vivo is still unknown. Mpr1 has been purified and crystallized in space groups P1 and P3(1)12. X-ray data were collected to 1.9 A resolution from a trigonal crystal soaked with AZC.
Hibi
Takao
T
Department of Bioscience, Fukui Prefectural University, Fukui 910-1195, Japan. hibi@fpu.ac.jp
Yamamoto
Hiromi
H
Nakamura
Genichi
G
Takagi
Hiroshi
H
D000123:Acetyltransferases / Q000737:chemistry* / Q000235:genetics; D000595:Amino Acid Sequence; D020134:Catalytic Domain / Q000235:genetics; D003460:Crystallization; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000235:genetics; D013379:Substrate Specificity / Q000235:genetics
D029701:Saccharomyces cerevisiae Proteins; D000123:Acetyltransferases; C492447:Mpr1 protein, S cerevisiae