Aminoacyl tRNA Synthetase: Difference between revisions
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<StructureSection load='' size='350' side='right' scene='44/444597/Cv/2' caption='Arginine tRNA synthetase complex with Arg-tRNA [[1f7v]]'> | <StructureSection load='' size='350' side='right' scene='44/444597/Cv/2' caption='Arginine tRNA synthetase complex with Arg-tRNA [[1f7v]]'> | ||
'''Aminoacyl tRNA synthetase''' (aaRS) or '''tRNA ligase''' 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).<ref>PMID:8422978</ref>. | '''Aminoacyl tRNA synthetase''' (aaRS) or '''aminoacyl tRNA ligase''' 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).<ref>PMID:8422978</ref>. | ||
*For '''leucine-RS''' details see [[Leucyl-tRNA Synthetase]]. | *For '''leucine-RS''' details see [[Leucyl-tRNA Synthetase]]. | ||
*For '''pyrrolysyl-RS''' of '''pyrrolysine-tRNA ligase''' details see [[Pyrrolysyl-tRNA synthetase]]. | *For '''pyrrolysyl-RS''' of '''pyrrolysine-tRNA ligase''' details see [[Pyrrolysyl-tRNA synthetase]]. | ||
Revision as of 11:34, 15 March 2021
Aminoacyl tRNA synthetase (aaRS) or aminoacyl tRNA ligase 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).[1].
3D Structures of Aminoacyl tRNA synthetaseAminoacyl tRNA synthetase 3D structures
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