Structure of an archaeal alanine:glyoxylate aminotransferase.
The crystal structure of a novel alanine:glyoxylate aminotransferase from the hyperthermophilic archaeon Thermococcus litoralis was determined at 2.3 A resolution. The asymmetric unit contains four homologous subunits and the functional tetramer is generated by noncrystallographic 222 symmetry. Although the main-chain coordinates of the monomer of the Thermococcus litoralis enzyme showed a high degree of similarity to those of aspartate aminotransferase from Thermus thermophilus HB8, the amino-acid residues involved in substrate binding in the aspartate aminotransferase are only partially conserved in the Thermococcus litoralis enzyme. This may account for the difference in the substrate specificities of the two enzymes.
Sakuraba
Haruhiko
H
Department of Life System, Institute of Technology and Science, The University of Tokushima, 2-1 Minamijosanjima-cho, Tokushima 770-8506, Japan.
Yoneda
Kazunari
K
Takeuchi
Kiyo
K
Tsuge
Hideaki
H
Katunuma
Nobuhiko
N
Ohshima
Toshihisa
T
D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D013045:Species Specificity; D013379:Substrate Specificity; D019712:Thermococcus / Q000201:enzymology* / Q000235:genetics; D016963:Thermus thermophilus / Q000201:enzymology / Q000235:genetics; D000637:Transaminases / Q000737:chemistry* / Q000235:genetics
D011994:Recombinant Proteins; D000637:Transaminases; C019635:Alanine-glyoxylate transaminase