Literature DB >> 1585461

Structural and functional relationships between aminoacyl-tRNA synthetases.

D Moras1.   

Abstract

Aminoacyl-tRNA synthetases can be divided in two groups of equal size on the basis of differences in the structure of their active sites. The core of class I synthetases is the classical nucleotide-binding domain with its characteristic Rossmann fold. In contrast, the active site of class II synthetases is built around an antiparallel beta-sheet, to which the substrates bind. This classification, which is based on structural data (amino acid sequences and tertiary structures), can be rationalized in functional terms.

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Year:  1992        PMID: 1585461     DOI: 10.1016/0968-0004(92)90326-5

Source DB:  PubMed          Journal:  Trends Biochem Sci        ISSN: 0968-0004            Impact factor:   13.807


  70 in total

1.  Assembly of a catalytic unit for RNA microhelix aminoacylation using nonspecific RNA binding domains.

Authors:  J W Chihade; P Schimmel
Journal:  Proc Natl Acad Sci U S A       Date:  1999-10-26       Impact factor: 11.205

2.  Emergence of template-and-sequence-directed (TSD) syntheses: I. A bio-geochemical model.

Authors:  N Lahav; S Nir
Journal:  Orig Life Evol Biosph       Date:  1997-08       Impact factor: 1.950

3.  Speculations on the evolution of the genetic code IV. The evolution of the aminoacyl-tRNA synthetases.

Authors:  H Hartman
Journal:  Orig Life Evol Biosph       Date:  1995-06       Impact factor: 1.950

4.  A mammalian homologue of GCN2 protein kinase important for translational control by phosphorylation of eukaryotic initiation factor-2alpha.

Authors:  R Sood; A C Porter; D A Olsen; D R Cavener; R C Wek
Journal:  Genetics       Date:  2000-02       Impact factor: 4.562

5.  Interstice mutations that block site-to-site translocation of a misactivated amino acid bound to a class I tRNA synthetase.

Authors:  Anthony C Bishop; Kirk Beebe; Paul R Schimmel
Journal:  Proc Natl Acad Sci U S A       Date:  2003-01-06       Impact factor: 11.205

6.  RNA binding determinant in some class I tRNA synthetases identified by alignment-guided mutagenesis.

Authors:  A Shepard; K Shiba; P Schimmel
Journal:  Proc Natl Acad Sci U S A       Date:  1992-10-15       Impact factor: 11.205

7.  Variant minihelix RNAs reveal sequence-specific recognition of the helical tRNA(Ser) acceptor stem by E.coli seryl-tRNA synthetase.

Authors:  M E Saks; J R Sampson
Journal:  EMBO J       Date:  1996-06-03       Impact factor: 11.598

8.  The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase.

Authors:  J G Arnez; J G Augustine; D Moras; C S Francklyn
Journal:  Proc Natl Acad Sci U S A       Date:  1997-07-08       Impact factor: 11.205

9.  The structural basis of cysteine aminoacylation of tRNAPro by prolyl-tRNA synthetases.

Authors:  Satwik Kamtekar; W Dexter Kennedy; Jimin Wang; Constantinos Stathopoulos; Dieter Söll; Thomas A Steitz
Journal:  Proc Natl Acad Sci U S A       Date:  2003-02-10       Impact factor: 11.205

10.  The presence of codon-anticodon pairs in the acceptor stem of tRNAs.

Authors:  S Rodin; A Rodin; S Ohno
Journal:  Proc Natl Acad Sci U S A       Date:  1996-05-14       Impact factor: 11.205

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