Modeling and analysis of the structure of the thermostable catechol 2,3-dioxygenase from Bacillus Stearothermophilus.
The three-dimensional structure of thermostable catechol 2,3-dioxygenase(TC230) from Bacillus Stearothermophilus has been modeled basing on the known x-ray structure of catechol 2,3-dioxygenase(metapyrocatechase) from Pseudomonas putida mt-2, using computer graphics energy minimization techniques. The rationality of the resulting model was validated by Ramachandran plot and Profile-3D. The structure-functionally important residues, such as M++ binding residues and the substrate binding residues, were identified from the model. These residues are candidates for further site-directed mutagenesis experiments. The reason that the thermostability of TC230 is greater than metapyrocatechase(MPC) has been found, which may be due to the specific structure of the TC230 in the C-end mainly.
Dai
L
L
Center of Analysis and Measurement, School of Life Sciences, Fudan University, Shanghai, China.
Ji
C
C
Gao
D
D
Wang
J
J
Jiang
T
T
Bi
A
A
Sheng
X
X
Mao
Y
Y
D000595:Amino Acid Sequence; D020134:Catalytic Domain; D050557:Catechol 2,3-Dioxygenase; D003198:Computer Simulation; D049308:Dioxygenases; D004795:Enzyme Stability; D001411:Geobacillus stearothermophilus / Q000201:enzymology* / Q000235:genetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010105:Oxygenases / Q000737:chemistry* / Q000235:genetics; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid; D013696:Temperature; D013816:Thermodynamics
D010105:Oxygenases; D049308:Dioxygenases; D050557:Catechol 2,3-Dioxygenase