Crystallization and preliminary X-ray diffraction analysis of thioredoxin peroxidase from the aerobic hyperthermophilic archaeon Aeropyrum pernix K1.
Thioredoxin peroxidase is a member of the peroxiredoxin family and plays a dominant role in a hydrogen peroxide metabolism. A recombinant form of the hyperthermostable thioredoxin peroxidase from the aerobic hyperthermophilic archaeon Aeropyrum pernix K1, a polypeptide consisting of 250 amino acids, was purified. The C207S mutant protein was crystallized by the hanging-drop vapour-diffusion method using potassium sodium tartrate as the precipitant at 298 K. Diffraction data were collected and processed to 2.7 A resolution. The crystal belongs to space group P1, with unit-cell parameters a = 126.2, b = 126.3, c = 213.7 A, alpha = 80.4, beta = 80.3, gamma = 70.7 degrees. Calculation of the self-rotation function showed that the protein quaternary structure includes a fivefold axis and five twofold axes.
Nakamura
Tsutomu
T
National Institute of Advanced Industrial Science and Technology, Ikeda, Osaka 563-8577, Japan. nakamura-t@aist.go.jp
Matsumura
Hiroyoshi
H
Inoue
Tsuyoshi
T
Kai
Yasushi
Y
Uegaki
Koichi
K
Hagihara
Yoshihisa
Y
Ataka
Mitsuo
M
Ishikawa
Kazuhiko
K
D041522:Aeropyrum / Q000201:enzymology*; D019843:Archaeal Proteins / Q000737:chemistry / Q000302:isolation & purification; D003001:Cloning, Molecular; D003460:Crystallization; D004926:Escherichia coli / Q000201:enzymology; D010544:Peroxidases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D054464:Peroxiredoxins; D020836:Protein Structure, Quaternary; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D014961:X-Ray Diffraction
D019843:Archaeal Proteins; D011994:Recombinant Proteins; D010544:Peroxidases; D054464:Peroxiredoxins