The solution structure of the S1 RNA binding domain: A member of an ancient nucleic acid-binding fold

被引：360

作者：

Bycroft, M ^{[1
]}

Hubbard, TJP ^{[1
]}

Proctor, M ^{[1
]}

Freund, SMV ^{[1
]}

Murzin, AG ^{[1
]}

机构：

[1] UNIV CAMBRIDGE, CTR MRC, CAMBRIDGE CB2 2QH, ENGLAND

来源：

CELL | 1997年 / 88卷 / 02期

基金：

英国医学研究理事会;

关键词：

D O I：

10.1016/S0092-8674(00)81844-9

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 S1 domain, originally identified in ribosomal protein S1, is found in a large number of RNA-associated proteins. The structure of the S1 RNA-binding domain from the E. coli polynucleotide phosphorylase has been determined using NMR methods and consists of a five-stranded antiparallel beta barrel. Conserved residues on one face of the barrel and adjacent loops form the putative RNA-binding site. The structure of the S1 domain is very similar to that of cold shock protein, suggesting that they are both derived from an ancient nucleic acid-binding protein. Enhanced sequence searches reveal hitherto unidentified S1 domains in RNase E, RNase II, NusA, EMB-5, and other proteins.

引用

页码：235 / 242

页数：8

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