Abstract
The selenomethionyl derivative of the thermostable catechol 2,3-dioxygenase (SeMet-TC23O) is expressed, purified and crystallized. By using multiwave length anomalous dispersion (MAD) phasing techniques, the crystal structure of TC23O at 0.3 nm resolutions is determined. TC23O is a homotetramer. Each monomer is composed of N-terminal and C-terminal domains (residues 1∼153 and 153∼319, respectively). The two domains are proximately symmetric by a non-crystallographic axis. Each domain contains two characteristic motifs which are found in almost all of extradial dioxygenases.
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References
Bertini, I., Briganti, F., Scozzafava, A., Aliphatic and aromatic inhibitors binding to the active site of catechol 2,3-dioxygenase from Pseudomonas putida mt-2, FEBS Letters, 1994, 343: 56.
Kang, B. S., Ha, J. Y., Lim, J. C. et al., Structure of catechol 2,3-dioxygenase gene from Alcaligenes eutrophus 335, Biochem. Biophys. Res. Commun., 1998, 245: 791.
Han, S., Eltis, L. D., Timmis, K. N. et al., Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading pseudomonad, Science, 1995, 270: 976.
Akiko, K., Shin-ichi, K., Ikuhide, F. et al., An archetypical extradiol-cleaving catecholic dioxygenase: The crystal structure of catechol 2,3-dioxygenase (metapyrocatechase) from Pseudomonas putida mt-2, Structure, 1999, 7: 25.
Duffner, F. M., Kirchner, U., Bauer, M. P. et al., Phenol/cresol degradation by the thermophilic Bacillus thermoglucosidasius A7: Cloning and sequence analysis of five genes involved in the pathway, Gene, 2000, 256: 215.
Hassett, D. J., Ochsner, U. A., Groce, S. L. et al., Hydrogen peroxide sensitivity of catechol-2,3-dioxygenase: A cautionary note on use of xylE reporter fusions under aerobic conditions, Appl. Environ. Microbiol., 2000, 66: 4119.
Dong, F. M., Wang, L. L., Wang, C. M. et al., Molecular cloning and mapping of phenol degradation genes from Bacillus stearothermophilus FDTP-3 and their expression in Escherichia coli, Appl. Environ. Microbiol., 1992, 58: 2531.
Zhang, W., Yin, C. C., Zheng, Z. H. et al., Overexpression, purification and characterization of thermostable catechol 2,3-dioxygenase, Acta Biochimica et Biophysica Sinica (in Chinese), 1998, 30: 579.
Chen, M. Q., Yin, C. C., Zhang, W. et al., Purification, crystallization and preliminary X-ray diffraction studies on the thermostable catechol 2,3-dioxygenase of Bacillus stearothermophilus expressed in Escherichia coli, Acta Cryst., 1998, D54: 446.
Kalick, S. E., Advances in multiple wavelength anomalous diffraction crystallography, Curr. Opin. Chem. Biol., 2000, 4: 495.
Hendrickson, W. A., Determination of macromolecular structures from anomalous diffraction of synchrotron radiation, Science, 1991, 254: 51.
Ogata, C., MAD phasing grows up, Nat. Struct. Biol., 1998, 5: 638.
Walsh, M., Dementieva, I., Evans, G. et al., Taking MAD to the extreme: Ultrafast protein structure determination, Acta Cryst., 1999, D55: 1168.
Sambrook, J., Fritsch, E. F., Maniatis, T., Molecular Cloning, 2nd ed., New York: Cold Spring Harbor Laboratory Press, 1989.
Ji, C. N., Jiang, T., Yin, C. C. et al., Expression and purification of Se-Met substituted thermostable catechol 2,3-dioxygenase, Journal of Fudan University (Natural Science), 2000, 3: 273.
Kita, A., Kita, S., Fujisawa, L. et al., An archetypical xetradiocleaving catecholic dioxygenase: The crystal structure of catechol 2,3-dioxygenase (metapyrocatechase) from Pseudomonas putida mt-2, Structure, 1999, 7: 25.
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Jiang, T., Ji, C., Sheng, X. et al. Crystal structure of thermostable catechol 2,3-dioxygenase determined by multiwavelength anomalous dispersion method. Chin.Sci.Bull. 47, 307–309 (2002). https://doi.org/10.1360/02tb9073
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DOI: https://doi.org/10.1360/02tb9073