Sandbox Reserved 704: Difference between revisions

From Proteopedia
Jump to navigationJump to search
No edit summary
No edit summary
Line 13: Line 13:
Leucyl-tRNA synthetase from the Archaeon Pyrococcus horikoshii is large (967 residues - 113kDa) and monomeric. LeuRS catalyses the esterification of tRNAs Leu with Leucine. There are two classes of aaRSs. Leucyl-tRNA synthetase (LeuRS) belong to the class I and more precisely to the class Ia. The class I enzymes have the Rossmann-fold domain (parallel β-sheet and α-helices) and the two characteristic motifs, with the consensus sequences of His-Ile-Gly-His (HIGH) and Lys-Met-Ser-Lys-Ser (KMSKS) This family is divided into prokaryotic and eukaryal/archaeal groups but we will focus on the second group.
Leucyl-tRNA synthetase from the Archaeon Pyrococcus horikoshii is large (967 residues - 113kDa) and monomeric. LeuRS catalyses the esterification of tRNAs Leu with Leucine. There are two classes of aaRSs. Leucyl-tRNA synthetase (LeuRS) belong to the class I and more precisely to the class Ia. The class I enzymes have the Rossmann-fold domain (parallel β-sheet and α-helices) and the two characteristic motifs, with the consensus sequences of His-Ile-Gly-His (HIGH) and Lys-Met-Ser-Lys-Ser (KMSKS) This family is divided into prokaryotic and eukaryal/archaeal groups but we will focus on the second group.


 
<Structure load='1wkb' size='500' frame='true' align='right' caption='1wkb' scene='Insert optional scene name here' />
<Structure load='1wkb' size='240' frame='true' align='right' caption="1wkb" scene=''>




Line 40: Line 39:




<StructureSection load='1wz2' size='350' side='right' caption='(PDB entry [[1wz2]])' scene=''>
<StructureSection load='1wz2' size='350' side='right' caption='(PDB entry [[1wz2]])' scene=''/>