CAVITIES IN PROTEINS - STRUCTURE OF A METMYOGLOBIN-XENON COMPLEX SOLVED TO 1.9-A
CAVITIES IN PROTEINS - STRUCTURE OF A METMYOGLOBIN-XENON COMPLEX SOLVED TO 1.9-A
复制标题
DOI：
10.1021/bi00308a002
复制
发表时间：
1984-01-01
期刊：
影响因子：
2.9
通讯作者：
PETSKO, GA
中科院分区：
文献类型：
--
作者：
TILTON, RF;KUNTZ, ID;PETSKO, GA
X射线晶体学数据为1.9-.在用7个大气压的氢气平衡的抹香鲸高铁肌红蛋白上收集分辨率。结果表明，在0.45-1.0之间有4个占位位点。这些位点位于肌红蛋白分子的内部空间或包装缺陷中。绑定的蛋白质结构的影响是轻微的，和一个小的整体减少，观察到在精制的各向同性原子蛋白质的温度因子。结果证实，在时间平均的基础上，腔存在于肌红蛋白分子内，并表明在这些腔中的小配体的结合影响蛋白质的内部运动和构象substates。
X-ray crystallographic data to 1.9-.ANG. resolution were collected on sperm whale metmyoglobin equilibrated with 7 atm of Xe gas. The results indicate 4 Xe sites of occupancy from 0.45-1.0. These sites are located in interior spaces or packing defects of the myoglobin molecule. The effects of the bound Xe on the protein structure are minor, and a small overall reduction is observed in refined isotropic atomic protein temperature factors. The results confirm that, on a time-averaged basis, cavities exist within the myoglobin molecule and suggest that the binding of small ligands in these cavities affects the internal motions and conformational substates of the protein.