核糖体结构之后：肽基转移酶是如何工作的？
After the ribosome structures: how does peptidyl transferase work?
作者信息
Moore Peter B, Steitz Thomas A
机构信息
Department of Chemistry, Howard Hughes Medical Institute, Yale University, 350 Edwards Street, New Haven, CT 06520-8107, USA.
出版信息
RNA. 2003 Feb;9(2):155-9. doi: 10.1261/rna.2127103.
Abstract
Atomic resolution crystal structures of the large subunit published since the middle of August 2000 prove that the peptidyl transferase center of the ribosome, which is the site of peptide-bond formation, is composed entirely of RNA; the ribosome is a ribozyme. They also demonstrate that alignment of the CCA ends of ribosome-bound peptidyl tRNA and aminoacyl tRNA in the peptidyl transferase center contributes significantly to its catalytic power. Several issues remain unresolved. For example, do any components of the site enhance the rate of peptide-bond formation chemically? Do intact ribosomes make peptide bonds the same way as the isolated large subunits that have been the source of all this atomic resolution structural information?
摘要
自2000年8月中旬以来发表的大亚基的原子分辨率晶体结构证明，核糖体的肽基转移酶中心（即肽键形成的位点）完全由RNA组成；核糖体是一种核酶。它们还表明，核糖体结合的肽基tRNA和氨酰tRNA的CCA末端在肽基转移酶中心的排列对其催化能力有显著贡献。几个问题仍未解决。例如，该位点的任何成分是否会在化学上提高肽键形成的速率？完整的核糖体形成肽键的方式与作为所有这些原子分辨率结构信息来源的分离大亚基相同吗？
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