DOMAINS OF ESCHERICHIA-COLI GLUTAMINYL-TRANSFER-RNA SYNTHETASE DISORDERED IN THE CRYSTAL-STRUCTURE ARE ESSENTIAL FOR FUNCTION OR STABILITY

被引：2

作者：

CONLEY, J ^{[1
]}

SHERMAN, J ^{[1
]}

THOMANN, HU ^{[1
]}

SOLL, D ^{[1
]}

机构：

[1] YALE UNIV,DEPT MOLEC BIOPHYS & BIOCHEM,NEW HAVEN,CT 06520

来源：

NUCLEOSIDES & NUCLEOTIDES | 1994年 / 13卷 / 6-7期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1080/15257779408012173

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：

Deletion analysis of E. coli glutaminyl-tRNA synthetase indicates that the N- and C-termini of the protein, which appear disordered in the crystal structure, are essential for function and stability in vivo. In vitro aminoacylation kinetics of a C-terminal deletion mutant exhibit a sharp reduction in the specificity constant. However, an N-terminal extension is catalytically, if not structurally equivalent to wild-type.

引用

页码：1581 / 1595

页数：15

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