EFFECTOR REGION OF THE TRANSLATION ELONGATION-FACTOR EF-TU GTP COMPLEX STABILIZES AN ORTHOESTER ACID INTERMEDIATE STRUCTURE OF AMINOACYL-TRANSFER-RNA IN A TERNARY COMPLEX

被引:16
作者
FORSTER, C [1 ]
LIMMER, S [1 ]
ZEIDLER, W [1 ]
SPRINZL, M [1 ]
机构
[1] UNIV BAYREUTH, BIOCHEM LAB, D-95440 BAYREUTH, GERMANY
关键词
C-13; NMR;
D O I
10.1073/pnas.91.10.4254
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
tRNA(Val) from Escherichia coli was aminoacylated with [1-C-13]valine and its complex with Thermus thermophilus elongation factor EF-Tu.GTP was analyzed by C-13 NMR spectroscopy. The results suggest that the aminoacyl residue of the valyl-tRNA in ternary complex with bacterial EF-Tu and GTP is not attached to tRNA by a regular ester bond to either a 2'- or 3' hydroxyl group; instead, an intermediate orthoester acid structure with covalent linkage to both vicinal hydroxyls of the terminal adenosine-76 is formed. Mutation of arginine-59 located in the effector region of EF-Tu, a conserved residue in protein elongation factors and the alpha subunits of heterotrimeric guanine nucleotide-binding regulatory proteins (G proteins), abolishes the stabilization of the orthoester acid structure of aminoacyl-tRNA.
引用
收藏
页码:4254 / 4257
页数:4
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