Darst S A
The Rockefeller University, Box 224, 1230 York Avenue, New York, NY 10021, USA.
Curr Opin Struct Biol. 2001 Apr;11(2):155-62. doi: 10.1016/s0959-440x(00)00185-8.
The recently determined crystal structure of a bacterial core RNA polymerase (RNAP) provides the first glimpse of this family of evolutionarily conserved cellular RNAPs. Using the structure as a framework, a consistent picture of protein-nucleic acid interactions in transcription complexes has been accumulated from cross-linking experiments. The molecule can be viewed as a molecular machine, with distinct structural features hypothesized to perform specific functions. Comparison with the alpha-carbon backbone of a eukaryotic RNAP reveals close structural similarity.
最近确定的一种细菌核心RNA聚合酶(RNAP)的晶体结构,首次让人们得以一窥这个进化上保守的细胞RNAP家族。以该结构为框架,通过交联实验积累了转录复合物中蛋白质与核酸相互作用的连贯图景。该分子可被视为一台分子机器,具有被假定执行特定功能的独特结构特征。与真核生物RNAP的α-碳骨架进行比较,发现结构上有密切的相似性。