Sandbox Reserved 704: Difference between revisions

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5) The <scene name='Sandbox_Reserved_704/Domain_5/1'>CP2 domain</scene> is inserted between the second and third β-sheets of the CP core. It is composed of a pair of antiparallel α-helices and a connecting β-sheet and is necessary for the amino acid activation and post-transfer editing.

6) ~~C-terminal domain and 7)~~ α-helix bundle domain ~~are essential for the tRNA binding throughout~~ the ~~tRNA Leu charging reaction. The~~ C-terminal ~~domain is important for the second step of the reaction, the transfer of the leucyl from the leucyl-adenylate to the 3’end of tRNA Leu. The α-helix bundle is found at the bottom~~ of the enzyme and consists of five long α-helices.

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.

8) LSD (Leucine-specific domain) 1 and 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) 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>.

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 29: / Line 29: @@
 ) The <scene name='Sandbox_Reserved_704/Domain_5/1'>CP2 domain</scene> is inserted between the second and third β-sheets of the CP core. It is composed of a pair of antiparallel α-helices and a connecting β-sheet and is necessary for the amino acid activation and post-transfer editing.
-) C-terminal domain and 7) α-helix bundle domain are essential for the tRNA binding throughout the tRNA Leu charging reaction. The C-terminal domain is important for the second step of the reaction, the transfer of the leucyl from the leucyl-adenylate to the 3’end of tRNA Leu. The α-helix bundle is found at the bottom of the enzyme and consists of five long α-helices.
+) 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 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>.
+) 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>.
 ) 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>.