Literature DB >> 12762019

Structural basis for amino acid and tRNA recognition by class I aminoacyl-tRNA synthetases.

O Nureki1, S Fukai, S Sekine, A Shimada, T Terada, T Nakama, M Shirouzu, D G Vassylyev, S Yokoyama.   

Abstract

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Year:  2001        PMID： 12762019     DOI： 10.1101/sqb.2001.66.167

Source DB:  PubMed          Journal:  Cold Spring Harb Symp Quant Biol        ISSN： 0091-7451


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  4 in total

1.  The 1.6 A crystal structure of Mycobacterium smegmatis MshC: the penultimate enzyme in the mycothiol biosynthetic pathway.

Authors:  L W Tremblay; F Fan; M W Vetting; J S Blanchard
Journal:  Biochemistry       Date:  2008-12-16       Impact factor: 3.162

2.  Substrate specificity of bacterial prolyl-tRNA synthetase editing domain is controlled by a tunable hydrophobic pocket.

Authors:  Sandeep Kumar; Mom Das; Christopher M Hadad; Karin Musier-Forsyth
Journal:  J Biol Chem       Date:  2011-11-29       Impact factor: 5.157

3.  Toward the catalytic mechanism of a cysteine ligase (MshC) from Mycobacterium smegmatis: an enzyme involved in the biosynthetic pathway of mycothiol.

Authors:  Fan Fan; John S Blanchard
Journal:  Biochemistry       Date:  2009-08-04       Impact factor: 3.162

4.  Paradox of mistranslation of serine for alanine caused by AlaRS recognition dilemma.

Authors:  Min Guo; Yeeting E Chong; Ryan Shapiro; Kirk Beebe; Xiang-Lei Yang; Paul Schimmel
Journal:  Nature       Date:  2009-12-10       Impact factor: 49.962
  4 in total

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