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
收藏
页码:1581 / 1595
页数:15
相关论文
共 44 条
[41]   SITE-DIRECTED MUTAGENESIS TO FINE-TUNE ENZYME SPECIFICITY [J].
UEMURA, H ;
ROGERS, MJ ;
SWANSON, R ;
WATSON, L ;
SOLL, D .
PROTEIN ENGINEERING, 1988, 2 (04) :293-296
[42]  
WALTER P, 1989, J BIOL CHEM, V264, P17126
[43]   SPECIFIC SEQUENCE HOMOLOGY AND 3-DIMENSIONAL STRUCTURE OF AN AMINOACYL TRANSFER-RNA SYNTHETASE [J].
WEBSTER, T ;
TSAI, H ;
KULA, M ;
MACKIE, GA ;
SCHIMMEL, P .
SCIENCE, 1984, 226 (4680) :1315-1317
[44]   THE STRUCTURE OF AN ANTIGENIC DETERMINANT IN A PROTEIN [J].
WILSON, IA ;
NIMAN, HL ;
HOUGHTEN, RA ;
CHERENSON, AR ;
CONNOLLY, ML ;
LERNER, RA .
CELL, 1984, 37 (03) :767-778