The three-dimensional structure of the ribosome and its components

被引：59

作者：

Moore, PB ^{[1
]}

机构：

[1] Yale Univ, Dept Chem, New Haven, CT 06520 USA

来源：

ANNUAL REVIEW OF BIOPHYSICS AND BIOMOLECULAR STRUCTURE | 1998年 / 27卷

关键词：

rRNA; ribosomal proteins; ribonucleoproteins; NMR; crystallography;

D O I：

10.1146/annurev.biophys.27.1.35

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：

Exciting progress has been made in the last decade by those who use physical methods to study the structure of the ribosome and its components. The structures of 10 ribosomal proteins and three isolated ribosomal protein domains are known, and the conformations of a significant number of rRNA sequences have been determined. Electron microscopists have made major advances in the analysis of images of ribosomes, and microscopically derived ribosome models at resolutions approaching 10 Angstrom are likely quite soon. Furthermore, ribosome crystallographers are on the verge of phasing the diffraction patterns they have had for several years, and near-atomic resolution models for entire ribosomal subunits could emerge from this source at any time. The literature relevant to these developments is reviewed below.

引用

页码：35 / 58

页数：24

共 109 条

[1] 3-DIMENSIONAL STRUCTURE OF THE RIBOSOMAL TRANSLOCASE - ELONGATION-FACTOR-G FROM THERMUS-THERMOPHILUS [J].