Ribosomal crystallography: a flexible nucleotide anchoring tRNA translocation facilitates peptide-bond formation, chirality discrimination and antibiotics synergism

被引：36

作者：

Agmon, I

Amit, M

Auerbach, T

Bashan, A

Baram, D

Bartels, H

Berisio, R

Greenberg, I

Harms, J

Hansen, HAS

Kessler, M

Pyetan, E

Schluenzen, F

Sittner, A

Yonath, A ^{[1
]}

Zarivach, R

机构：

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

[2] Max Planck Res Unit Ribosomal Struct, D-22603 Hamburg, Germany

来源：

FEBS LETTERS | 2004年 / 567卷 / 01期

关键词：

ribosome; peptide-bond formation; positional catalysis; antibiotics synergism; synercid; azithromycin; dual binding;

D O I：

10.1016/j.febslet.2004.03.065

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：

The linkage between internal ribosomal symmetry and transfer RNA (tRNA) positioning confirmed positional catalysis of amino-acid polymerization. Peptide bonds are formed concurrently with tRNA-3' end rotatory motion, in conjunction with the overall messenger RNA (mRNA)/tRNA translocation. Accurate substrate alignment, mandatory for the processivity of protein biosynthesis, is governed by remote interactions. Inherent flexibility of a conserved nucleotide, anchoring the rotatory motion, facilitates chirality discrimination and antibiotics synergism. Potential tRNA interactions explain the universality of the tRNA CCA-end and P-site preference of initial tRNA. The interactions of protein L2 tail with the symmetry-related region periphery explain its conservation and its contributions to nascent chain elongation. (C) Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.

引用

页码：20 / 26

页数：7