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- W752015704 abstract "This chapter reviews the recognition specificity of a class II aminoacyl-tRNA synthetases (aaRS) and AspRS in detail. Class II aaRS are characterized by three signature motifs, each containing strictly conserved residues. The crystal structures of SerRS from Escherichia coli and AspRS from yeast gave a clear structural explanation for the partition into the two classes. Indeed, class II aaRS contain a new fold, consisting of an antiparallel β sheet flanked by two α helices. The structures of the complex formed by tRNAAsp and AspRS from yeast, with or without ATP correlate these motifs with their biological function; highly conserved residues from motifs 2 and 3 are responsible for ATP binding. Seven class II aaRS exhibit motifs 1 , 2 , and 3. More stringent sequence homology requirements led to the definition of subclasses. Class IIc aaRS (GlyRS, AlaRS, and PheRS) do not contain motif 1 and have a different quaternary organization. PheRS is an even more special case because it has the motif 2 and 3 characteristics of class II but behaves like a class I synthetase as to its primary site of aminoacylation." @default.
- W752015704 created "2016-06-24" @default.
- W752015704 creator A5010706989 @default.
- W752015704 creator A5016465734 @default.
- W752015704 date "2014-04-30" @default.
- W752015704 modified "2023-10-17" @default.
- W752015704 title "The Aspartic Acid tRNA System: Recognition by a Class II Aminoacyl-tRNA Synthetase" @default.
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- W752015704 doi "https://doi.org/10.1128/9781555818333.ch20" @default.
- W752015704 hasPublicationYear "2014" @default.
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