Crystal structure analysis of omega-amino acid:pyruvate aminotransferase with a newly developed Weissenberg camera and an imaging plate using synchrotron radiation.
The three-dimensional structure of omega-amino acid:pyruvate aminotransferase from Pseudomonas sp. F-126, an isologous alpha 4 tetramer containing pyridoxal 5'-phosphate (PLP) as a cofactor, has been determined at 2.0 A resolution. The diffraction data were collected with a newly developed Weissenberg camera with a Fuji Imaging Plate, using synchrotron radiation. The mean figure-of-merit was 0.57. The subunit is rich in secondary structure and comprises two domains. PLP is located in the large domain. The high homology in the secondary structure between this enzyme and aspartate aminotransferase strongly indicates that these two types of enzymes have evolved from a common ancestor.
Watanabe
N
N
Institute of Physics, University of Tsukuba, Ibaraki.
Sakabe
K
K
Sakabe
N
N
Higashi
T
T
Sasaki
K
K
Aibara
S
S
Morita
Y
Y
Yonaha
K
K
Toyama
S
S
Fukutani
H
H
D001219:Aspartate Aminotransferases; D003461:Crystallography; D011487:Protein Conformation; D011550:Pseudomonas aeruginosa / Q000201:enzymology; D011732:Pyridoxal Phosphate; D011877:Radionuclide Imaging; D000637:Transaminases; D051278:beta-Alanine-Pyruvate Transaminase
D011732:Pyridoxal Phosphate; D000637:Transaminases; D001219:Aspartate Aminotransferases; D051278:beta-Alanine-Pyruvate Transaminase