Moore Peter B, Steitz Thomas A
Departments of Molecular Biophysics and Biochemistry, Chemistry, Yale University, New Haven, Connecticut 06520, USA.
Annu Rev Biochem. 2003;72:813-50. doi: 10.1146/annurev.biochem.72.110601.135450.
The ribosome crystal structures published in the past two years have revolutionized our understanding of ribonucleoprotein structure, and more specifically, the structural basis of the peptide bonding forming activity of the ribosome. This review concentrates on the crystallographic developments that made it possible to solve these structures. It also discusses the information obtained from these structures about the three-dimensional architecture of the large ribosomal subunit, the mechanism by which it facilitates peptide bond formation, and the way antibiotics inhibit large subunit function. The work reviewed, taken as a whole, proves beyond doubt that the ribosome is an RNA enzyme, as had long been surmised on the basis of less conclusive evidence.
过去两年发表的核糖体晶体结构彻底改变了我们对核糖核蛋白结构的理解，更具体地说，是对核糖体肽键形成活性的结构基础的理解。本综述集中于使解析这些结构成为可能的晶体学进展。它还讨论了从这些结构中获得的有关大核糖体亚基三维结构、其促进肽键形成的机制以及抗生素抑制大亚基功能的方式的信息。整体来看，所综述的这项研究确凿无疑地证明核糖体是一种RNA酶，正如长期以来基于不太确凿的证据所推测的那样。
