Crystal structure of the TK2203 protein from Thermococcus kodakarensis, a putative extradiol dioxygenase.
The TK2203 protein from the hyperthermophilic archaeon Thermococcus kodakarensis KOD1 (262 residues, 29 kDa) is a putative extradiol dioxygenase catalyzing the cleavage of C-C bonds in catechol derivatives. It contains three metal-binding residues, but has no significant sequence similarity to proteins for which structures have been determined. Here, the first crystal structure of the TK2203 protein was determined at 1.41 Å resolution to investigate its functional role. Structure analysis reveals that this protein shares the same fold and catalytic residues as other extradiol dioxygenases, strongly suggesting the same enzymatic activity. Furthermore, the important region contributing to substrate selectivity is discussed.
Department of Chemistry, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
Yuichi
Y
Nishitani
Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Katsura, Nishikyo-ku, Kyoto 615-8510, Japan.
Jan Robert
JR
Simons
Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Katsura, Nishikyo-ku, Kyoto 615-8510, Japan.
Tamotsu
T
Kanai
Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Katsura, Nishikyo-ku, Kyoto 615-8510, Japan.
Haruyuki
H
Atomi
Department of Chemistry, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
Kunio
K
Miki
D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D010105:Oxygenases / Q000737:chemistry*; D011487:Protein Conformation; D019712:Thermococcus / Q000737:chemistry*
D010105:Oxygenases; C439587:extradiol dioxygenase
SIRAS; TK2203; Thermococcus kodakarensis; archaea; aromatic compound degradation; homodimer; nonhaem iron