Aminoacyl tRNA Synthetase
From Proteopedia
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*''Leu-RS ternary complex''<br /> | *''Leu-RS ternary complex''<br /> | ||
| + | **[[2v0g]] - TtLeuRS + Leu-tRNA + benzoxaborole-AMP<br /> | ||
**[[2bte]], [[ 2byt]] - TtLeuRS + Leu-tRNA + Leu | **[[2bte]], [[ 2byt]] - TtLeuRS + Leu-tRNA + Leu | ||
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**[[2dxi]] – TtMetRS + tRNA + ATP + Glu-ol | **[[2dxi]] – TtMetRS + tRNA + ATP + Glu-ol | ||
| + | *''Met-RS coplex''<br /> | ||
| + | |||
| + | **[[4bl7]], [[4bvx]], [[4bvy]] - hMetRS N-terminal + elongation factor P18<br /> | ||
**[[2hsn]] - yMetRS N-terminal + GU4 nucleic-binding protein 1 N-terminal | **[[2hsn]] - yMetRS N-terminal + GU4 nucleic-binding protein 1 N-terminal | ||
Revision as of 12:38, 28 January 2015
Aminoacyl tRNA synthetase (aaRS) catalyzes the esterification of a specific amino acid to its cognate tRNA to form an aminoacyl-tRNA. The amino acid is transferred by the ribosome from the aminoacylated-tRNA onto a growing polypeptide chain. Class I of aaRS is a monomer or dimer, it has 2 highly conserved sequence motifs and it aminoacylates at the 2’-OH of an adenosine nucleotide. Class II of aaRS is a dimer or tetramer, it has 3 highly conserved sequence motifs and it aminoacylates at the 3’-OH of an adenosine nucleotide. CP1 domain of RS edits a mischarged aa-tRNA. Some of the crystal structures are complexes of the RS with their reactant analog: amino acid-sulfamoyl adenine (aa-SA).
3D Structures of Aminoacyl tRNA synthetase
Updated on 28-January-2015
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Joel L. Sussman, Ann Taylor
