通过与其他X射线结构进行同源性分析来构建嗜热栖热菌红素氧化还原蛋白的结构模型。
Modeling the structure of Pyrococcus furiosus rubredoxin by homology to other X-ray structures.
作者信息
Wampler J E, Bradley E A, Stewart D E, Adams M W
机构信息
Department of Biochemistry, University of Georgia, Athens 30602.
出版信息
Protein Sci. 1993 Apr;2(4):640-9. doi: 10.1002/pro.5560020414.
The three-dimensional structure of rubredoxin from the hyperthermophilic archaebacterium, Pyrococcus furiosus, has been modeled from the X-ray crystal structures of three homologous proteins from Clostridium pasteurianum, Desulfovibrio gigas, and Desulfovibrio vulgaris. All three homology models are similar. When comparing the positions of all heavy atoms and essential hydrogen atoms to the recently solved crystal structure (Day, M. W., et al., 1992, Protein Sci. 1, 1494-1507) of the same protein, the homology model differ from the X-ray structure by 2.09 A root mean square (RMS). The X-ray and the zinc-substituted NMR structures (Blake, P. R., et al., 1992b, Protein Sci. 1, 1508-1521) show a similar level of difference (2.05 A RMS). On average, the homology models are closer to the X-ray structure than to the NMR structures (2.09 vs. 2.42 A RMS).
嗜热古细菌激烈火球菌（Pyrococcus furiosus）中红氧还蛋白的三维结构已根据来自巴氏梭菌（Clostridium pasteurianum）、巨大脱硫弧菌（Desulfovibrio gigas）和普通脱硫弧菌（Desulfovibrio vulgaris）的三种同源蛋白质的X射线晶体结构进行了建模。所有这三种同源性模型都很相似。当将所有重原子和必需氢原子的位置与最近解析的同一蛋白质的晶体结构（Day, M. W., 等人，1992年，《蛋白质科学》1, 1494 - 1507）进行比较时，同源性模型与X射线结构的均方根（RMS）差异为2.09 Å。X射线结构与锌取代的核磁共振结构（Blake, P. R., 等人，1992b年，《蛋白质科学》1, 1508 - 1521）显示出相似水平的差异（2.05 Å RMS）。平均而言，同源性模型更接近X射线结构而非核磁共振结构（均方根分别为2.09 Å和2.42 Å）。
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