This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Aminoacyl tRNA Synthetase
From Proteopedia
| Line 544: | Line 544: | ||
**[[1fyj]] – hRS - NMR | **[[1fyj]] – hRS - NMR | ||
}} | }} | ||
| - | + | == References == | |
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 09:04, 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
References
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Joel L. Sussman, Ann Taylor
