Ribosome crystallography: catalysis and evolution of peptide-bond formation., nascent chain elongation and its co-translational folding

被引：15

作者：

Bashan, A ^{[1
]}

Yonath, A ^{[1
]}

机构：

[1] Weizmann Inst Sci, Dept Biol Struct, IL-76100 Rehovot, Israel

来源：

BIOCHEMICAL SOCIETY TRANSACTIONS | 2005年 / 33卷

关键词：

nascent chain elongation; peptide-bond formation; positional analysis; ribosome substrate-mediated catalysis; trigger factor;

D O I：

10.1042/BST0330488

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A ribosome is a ribozyme polymerizing amino acids, exploiting positional- and substrate-mediated chemical catalysis. We showed that peptide-bond formation is facilitated by the ribosomal architectural frame, provided by a sizable symmetry-related region in and around the peptidyl transferase centre, suggesting that the ribosomal active site was evolved by gene fusion. Mobility in tunnel components is exploited for elongation arrest as well as for trafficking nascent proteins into the folding space bordered by the bacterial chaperone, namely the trigger factor.

引用

页码：488 / 492

页数：5

共 33 条

[11]

Dall'Acqua W, 2000, PROTEIN SCI, V9, P1

[12] The dynamic tunnel [J].