Sandbox Reserved 704: Difference between revisions
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{{Sandbox_ESBS_2012}} | {{Sandbox_ESBS_2012}} | ||
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=== Crystal structure of leucyl-tRNA synthetase and tRNA (leucine) complex === | === Crystal structure of leucyl-tRNA synthetase and tRNA (leucine) complex === | ||
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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='500' frame='true' align='right' caption='1wkb: Crystal Structure of Leucyl-tRNA Synthetase from the Archaeon Pyrococcus horikoshii [[resolution 2.05Å]] ' scene='Insert optional scene name here' /> | ||
