Dai L, Ji C, Gao D, Wang J, Jiang T, Bi A, Sheng X, Mao Y
Center of Analysis and Measurement, School of Life Sciences, Fudan University, Shanghai, China.
J Biomol Struct Dyn. 2001 Aug;19(1):75-83. doi: 10.1080/07391102.2001.10506721.
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.
基于嗜热脂肪芽孢杆菌的热稳定儿茶酚2,3-双加氧酶（TC230）的三维结构，利用计算机图形能量最小化技术，依据恶臭假单胞菌mt-2的儿茶酚2,3-双加氧酶（间苯二酚酶）已知的X射线结构进行了建模。通过拉氏图和Profile-3D验证了所得模型的合理性。从该模型中鉴定出了结构功能上重要的残基，如M++结合残基和底物结合残基。这些残基是进一步定点诱变实验的候选对象。已经发现TC230的热稳定性高于间苯二酚酶（MPC）的原因，这可能主要归因于TC230在C端的特定结构。
