核糖体催化肽键形成机制的结构观点。
A structural view on the mechanism of the ribosome-catalyzed peptide bond formation.
作者信息
Simonović Miljan, Steitz Thomas A
机构信息
Department of Biochemistry and Molecular Genetics, University of Illinois at Chicago, MBRB 1170, 900 S Ashland Ave., Chicago, IL 60607, USA.
出版信息
Biochim Biophys Acta. 2009 Sep-Oct;1789(9-10):612-23. doi: 10.1016/j.bbagrm.2009.06.006. Epub 2009 Jul 9.
Abstract
The ribosome is a large ribonucleoprotein particle that translates genetic information encoded in mRNA into specific proteins. Its highly conserved active site, the peptidyl-transferase center (PTC), is located on the large (50S) ribosomal subunit and is comprised solely of rRNA, which makes the ribosome the only natural ribozyme with polymerase activity. The last decade witnessed a rapid accumulation of atomic-resolution structural data on both ribosomal subunits as well as on the entire ribosome. This has allowed studies on the mechanism of peptide bond formation at a level of detail that surpasses that for the classical protein enzymes. A current understanding of the mechanism of the ribosome-catalyzed peptide bond formation is the focus of this review. Implications on the mechanism of peptide release are discussed as well.
摘要
核糖体是一种大型核糖核蛋白颗粒，它将mRNA中编码的遗传信息翻译成特定的蛋白质。其高度保守的活性位点，即肽基转移酶中心（PTC），位于大（50S）核糖体亚基上，仅由rRNA组成，这使得核糖体成为唯一具有聚合酶活性的天然核酶。在过去十年中，关于核糖体亚基以及整个核糖体的原子分辨率结构数据迅速积累。这使得对肽键形成机制的研究达到了超越经典蛋白质酶的详细程度。本文综述聚焦于目前对核糖体催化肽键形成机制的理解。同时也讨论了对肽释放机制的影响。
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