| Interacting proteins: P26640 and P41252 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P26640 and P41252 |
Pubmed |
SVM Score :0.0 |
| Out of the 18 known aaRS , only 9 referred to as class 1 synthetases ( GlnRS , TyrRS , MetRS , GluRS , ArgRS , ValRS , IleRS , LeuRS , TrpRS ) , display two short common consensus sequences ( ' HIGH ' and ' KMSKS ' ) which indicate , as observed in three crystal structures , the presence of a structural domain ( the Rossman fold ) that binds ATP . ^^^ |
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| Interacting proteins: P26640 and P41252 |
Pubmed |
SVM Score :0.0 |
| The alignments also indicate that the class 1 synthetases may be partitioned into two subgroups : a ) MetRS , IleRS , LeuRS , ValRS , CysRS and ArgRS ; b ) GlnRS , GluRS , TyrRS and TrpRS . . ^^^ |
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| Interacting proteins: P26640 and P41252 |
Pubmed |
SVM Score :0.0 |
| For example , the close homologs isoleucyl tRNA synthetase ( IleRS ) and valyl tRNA synthetase ( ValRS ) deacylate Val tRNA ( Ile ) and Thr tRNA ( Val ) , respectively . ^^^ |
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| Interacting proteins: P26640 and P41252 |
Pubmed |
SVM Score :0.0 |
| For isoleucyl ( IleRS ) and valyl tRNA synthetases ( ValRS ) , reactions that hydrolyze misactivated noncognate amino acids help to achieve high accuracy in aminoacylation . ^^^ |
|
| Interacting proteins: P26640 and P41252 |
Pubmed |
SVM Score :0.0 |
| The editing domains of the closely homologous leucyl , isoleucyl , and valyl tRNA synthetases ( LeuRS , IleRS , and ValRS , respectively ) contribute to accurate aminoacylation , by hydrolyzing misformed non cognate aminoacyl tRNAs . ^^^ The editing domain is inserted at the same point of the sequence in IleRS , ValRS , and the archaeal / eukaryal LeuRS , but at a distinct point in the bacterial LeuRS . ^^^ The editing domain of P . horikoshii LeuRS is rotated by approximately 180 degrees ( rotational state 2 ) , with the two beta stranded linker untwisted by a half turn , as compared to those in IleRS and ValRS ( rotational state 1 ) . ^^^ Thus , we established that there are three types of editing domain orientations relative to the enzyme core , depending on the combination of the editing domain insertion point ( 1 or 2 ) and the rotational state ( 1 or 2 ) : [ 1 , 1 ] for IleRS and ValRS , [ 2 , 2 ] for the bacterial LeuRS , and now [ 1 , 2 ] for the archaeal / eukaryal LeuRS . . ^^^ |
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| Interacting proteins: P26640 and P41252 |
Pubmed |
SVM Score :0.0 |
| Although this appears to be consistent with an editing mechanism in which there is a slow transfer of the valine from the IRS Val AMP to tRNAIle follwed by the rapid hydrolytic step , as recently found for the rejection of threonine by the valyl tRNA synthetase , there is an inconsistency . ^^^ |
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| Interacting proteins: P26640 and P41252 |
Pubmed |
SVM Score :0.0 |
| Aminoacyl tRNA synthetases of bakers ' yeast ( Saccharomyces cerevisiae ) were adsorbed to a phosphocellulose ( P cellulose ) column , and those specific for tyrosine [ EC 6 . 1 . 1 . 1 ] , threonine [ EC 6 . 1 . 1 . 3 ] , valine [ EC 6 . 1 . 1 . 9 ] , and isoleucine [ EC 6 . 1 . 1 . 5 ] were eluted with several specific tRNAs . ^^^ |
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