Sinning I, Koepke J, Schiller B, Michel H
Max-Planck-Institut für Biophysik, Frankfurt, Bundesrepublik Deutschland.
Z Naturforsch C J Biosci. 1990 May;45(5):455-8. doi: 10.1515/znc-1990-0525.
A first model of the three-dimensional structure of the photosynthetic reaction center of the mutant T1 (SerL223----Ala, ArgL217----His) from Rhodopseudomonas viridis, resistant toward the triazine herbicide terbutryn (2-methylthio-4-ethylamino-6-t-butylamino-s-triazine), has been developed from X-ray data measured to a resolution of 2.5 A. The secondary quinone, QB, which in T1 binds better than in the wild type, is present in the crystals. Both substituted residues are clearly visible in the difference fourier map. The replacement of these two residues in the QB site causes only minor changes in the overall structure of the protein.
已根据分辨率为2.5埃的X射线数据构建了来自绿硫红假单胞菌的对三嗪除草剂特丁净（2-甲硫基-4-乙氨基-6-叔丁氨基-s-三嗪）具有抗性的突变体T1（SerL223→Ala，ArgL217→His）光合反应中心的三维结构的首个模型。晶体中存在二级醌QB，其在T1中的结合比野生型更好。在差值傅里叶图中，两个取代的残基清晰可见。QB位点这两个残基的替换仅导致蛋白质整体结构发生微小变化。
