Sandbox Reserved 704: Difference between revisions

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6) The <scene name='Sandbox_Reserved_704/Domain_6/1'>α-helix bundle domain</scene> is found at the C-terminal end of the enzyme and consists of five long α-helices. It is essential for the tRNA binding throughout the tRNA Leu charging reaction.

7) LSD (Leucine-specific domain) 1 and 8) LSD2 have been described in Archaeal LeuRs, inserted between the two helices in Rossmann-fol domain. They vary in size. LSD1 is a small domain which includes two antiparallel α-helices. The crystal structure of the apo enzyme suggests that LSD1 may have the potential to regulate the KMSKS loop opening and closing. This loop is highly dynamic and flexible during amino acid activation. LSD2 is a large domain (5 bundle α-helices) located on the opposite site of the enzyme relative to the aminoacylation active site <ref name="Zhou">PMID:20482517</ref>.

7) The <scene name='Sandbox_Reserved_704/Lsd1/1'>LSD (Leucine-specific domain) 1</scene> and 8) LSD2 have been described in Archaeal LeuRs, inserted between the two helices in Rossmann-fol domain. They vary in size. LSD1 is a small domain which includes two antiparallel α-helices. The crystal structure of the apo enzyme suggests that LSD1 may have the potential to regulate the KMSKS loop opening and closing. This loop is highly dynamic and flexible during amino acid activation. LSD2 is a large domain (5 bundle α-helices) located on the opposite site of the enzyme relative to the aminoacylation active site <ref name="Zhou">PMID:20482517</ref>.

9) SC-fold domain follows the Rossmann-fold domain. His β-α-α-β-α topology is characteristic. It contains the KMSKS motif, which is located on the loop between the first β-sheet and the first α-helix of its topology <ref name="Fukunaga">PMID:15663927</ref>.

Sandbox Reserved 704: Difference between revisions

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@@ Line 31: / Line 31: @@
 ) The <scene name='Sandbox_Reserved_704/Domain_6/1'>α-helix bundle domain</scene> is found at the C-terminal end of the enzyme and consists of five long α-helices. It is essential for the tRNA binding throughout the tRNA Leu charging reaction.
-) LSD (Leucine-specific domain) 1 and 8) LSD2 have been described in Archaeal LeuRs, inserted between the two helices in Rossmann-fol domain. They vary in size. LSD1 is a small domain which includes two antiparallel α-helices. The crystal structure of the apo enzyme suggests that LSD1 may have the potential to regulate the KMSKS loop opening and closing. This loop is highly dynamic and flexible during amino acid activation. LSD2 is a large domain (5 bundle α-helices) located on the opposite site of the enzyme relative to the aminoacylation active site <ref name="Zhou">PMID:20482517</ref>.
+) The <scene name='Sandbox_Reserved_704/Lsd1/1'>LSD (Leucine-specific domain) 1</scene> and 8) LSD2 have been described in Archaeal LeuRs, inserted between the two helices in Rossmann-fol domain. They vary in size. LSD1 is a small domain which includes two antiparallel α-helices. The crystal structure of the apo enzyme suggests that LSD1 may have the potential to regulate the KMSKS loop opening and closing. This loop is highly dynamic and flexible during amino acid activation. LSD2 is a large domain (5 bundle α-helices) located on the opposite site of the enzyme relative to the aminoacylation active site <ref name="Zhou">PMID:20482517</ref>.
 ) SC-fold domain follows the Rossmann-fold domain. His β-α-α-β-α  topology is characteristic. It contains the KMSKS motif, which is located on the loop between the first β-sheet and the first α-helix of its topology <ref name="Fukunaga">PMID:15663927</ref>.