An intermediate step in the recognition of tRNAAsp by Aspartyl-tRNA synthetase

被引：40

作者：

Briand, C ^{[1
]}

Poterszman, A ^{[1
]}

Eiler, S ^{[1
]}

Webster, G ^{[1
]}

Thierry, JC ^{[1
]}

Moras, D ^{[1
]}

机构：

[1] ULP, INSERM, CNRS, IGBMC,Lab Biol & Geonom,UPR 9004, F-67404 Illkirch Graffenstaden, France

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2000年 / 299卷 / 04期

关键词：

class II aminoacyl-tRNA synthetase; Thermus thermophilus aspartyl-tRNA synthetase; Thermus thermophilus tRNA(Asp); Escherichia coli tRNA(Asp); crystal structure;

D O I：

10.1006/jmbi.2000.3819

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 crystal structures of aspartyl-tRNA synthetase (AspRS) from Thermus thermophilus, a prokaryotic class IIb enzyme, complexed with tRNA(Asp) from either T. thermophilus or Escherichia coli reveal a potential intermediate of the recognition process. The tRNA is positioned on the enzyme such that it cannot be aminoacylated but adopts an overall conformation similar to that observed in active complexes. While the anticodon loop binds to the N-terminal domain of the enzyme in a manner similar to that of the related active complexes, its aminoacyl acceptor arm remains at the entrance of the active site, stabilized in its intermediate conformational state by non-specific interactions with the insertion and catalytic domains. The thermophilic nature of the enzyme, which manifests itself in a very low kinetic efficiency at 17 degrees C, the temperature at which the crystals were grown, is in agreement with the relative stability of this non-productive conformational state. Based on these data, a pathway for tRNA binding and recognition is proposed. (C) 2000 Academic Press.

引用

页码：1051 / 1060

页数：10