Ke H M, Honzatko R B, Lipscomb W N
Proc Natl Acad Sci U S A. 1984 Jul;81(13):4037-40. doi: 10.1073/pnas.81.13.4037.
The three-dimensional structure of the allosteric enzyme aspartate carbamoyltransferase (EC 2.1.3.2) has been refined to a crystallographic R-factor of 0.24 at 2.6-A resolution in the space group P321, where a and b are 122.1 A and c is 142.2 A. This structure is isomorphous to the form of the enzyme complexed to the allosteric inhibitor cytidine triphosphate. All sources of sequence information have been evaluated against the electron density. The corrected amino acid sequences of the catalytic and regulatory proteins have been incorporated in the model, and three regions in the active site are described: (i) near arginine-105, histidine-134, and arginine-167, (ii) near lysine-232 and arginine-229, and (iii) near lysine-83 and lysine-84.
变构酶天冬氨酸氨甲酰基转移酶(EC 2.1.3.2)的三维结构在空间群P321中已精修至2.6埃分辨率下晶体学R因子为0.24,其中a和b为122.1埃,c为142.2埃。该结构与和变构抑制剂三磷酸胞苷复合的酶形式同晶型。已根据电子密度评估了所有序列信息来源。催化蛋白和调节蛋白的校正氨基酸序列已纳入模型,并描述了活性位点的三个区域:(i)靠近精氨酸-105、组氨酸-134和精氨酸-167处,(ii)靠近赖氨酸-232和精氨酸-229处,以及(iii)靠近赖氨酸-83和赖氨酸-84处。