Ribosomal proteins and elongation factors

被引：55

作者：

Liljas, A ^{[1
]}

Garber, M ^{[1
]}

机构：

[1] RUSSIAN ACAD SCI, INST PROT RES, PUSHCHINO 142292, RUSSIA

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 1995年 / 5卷 / 06期

关键词：

D O I：

10.1016/0959-440X(95)80003-4

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：

Structural work on the translation machinery has recently undergone rapid progress. It is now known that six out of nine ribosomal proteins have an RNA-binding fold, and two domains of elongation factors Tu and G have very similar folds. in addition, the complex of EF-Tu with a GTP analogue and Phe-tRNA(Phe) has a structure that overlaps exceedingly well with that of EF-G GDP. These findings obviously have functional implications.

引用

页码：721 / 727

页数：7

共 59 条

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