Aminoacyl tRNA Synthetase
From Proteopedia
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[[Image:3l4g.png|left|200px|thumb|Crystal Structure of Aminoacyl tRNA synthetase [[3l4g]]]] | [[Image:3l4g.png|left|200px|thumb|Crystal Structure of Aminoacyl tRNA synthetase [[3l4g]]]] | ||
| - | {{STRUCTURE_1f7v| PDB=1f7v | SIZE= | + | {{STRUCTURE_1f7v| PDB=1f7v | SIZE=350| SCENE=|right|CAPTION=Arginine tRNA synthetase complex with Arg-tRNA [[1f7v]] }} |
Revision as of 09:03, 2 December 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). For pyrrolysyl-RS details see Pyrrolysyl-tRNA synthetase.
3D Structures of Aminoacyl tRNA synthetase
Updated on 02-December-2015
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Joel L. Sussman, Ann Taylor
