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PMID: 1585461 Published · ppublish English Journal Article Review

Structural and functional relationships between aminoacyl-tRNA synthetases.

Trends in biochemical sciences ·Vol. 17 ·No. 4 ·1992-04-00 ·Pages 159-64

Moras D

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.

MeSH Terms
Amino Acyl-tRNA Synthetases/chemistry,classification,metabolism Biological Evolution Protein Conformation RNA, Transfer/metabolism Sequence Homology, Nucleic Acid Structure-Activity Relationship
Chemicals
RNA, Transfer Amino Acyl-tRNA Synthetases
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Moras D
Institut de Biologie, Moléculaire et Cellulaire du CNRS, Laboratoire de Cristallographie Biologique, Strasbourg, France.
Article Info
Journal
Trends in biochemical sciences
Abbr.
Trends Biochem Sci
ISSN
0968-0004
Published
1992-04-00
Pages
159-64
Language
English
Region
England
NLM ID
7610674
Subset
IM
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