Sandbox Reserved 704: Difference between revisions

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The structure can be divided into nine domains <ref name="Fukunaga">PMID:15663927</ref> :

1) The class I-characterizing <scene name='Sandbox_Reserved_704/Domain_1/1'>Rossmann-fold aminoacylation catalytic domain</scene>: It contains the HIGH motif. It is located at the beginning of the long α-helix found below the Rossmann-fold core β-sheet.

1) The class I-characterizing <scene name='Sandbox_Reserved_704/Domain_1/2'>Rossmann-fold aminoacylation catalytic domain</scene>: It contains the HIGH motif. It is located at the beginning of the long α-helix found below the Rossmann-fold core β-sheet.

Other the Rossmann fold domain, there are other fused and inserted domains:

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7) The <scene name='Sandbox_Reserved_704/Lsd1/1'>LSD (Leucine-specific domain) 1</scene> and 8) <scene name='Sandbox_Reserved_704/Domain_8/1'>LSD2</scene> 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) The <scene name='Sandbox_Reserved_704/Domain_9/1'>SC-fold domain</scene>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>.

9) The <scene name='Sandbox_Reserved_704/Domain_9/1'>SC-fold domain</scene> 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 20: / Line 20: @@
 The structure can be divided into nine domains <ref name="Fukunaga">PMID:15663927</ref> :
-) The class I-characterizing <scene name='Sandbox_Reserved_704/Domain_1/1'>Rossmann-fold aminoacylation catalytic domain</scene>: It contains the HIGH motif. It is located at the beginning of the long α-helix found below the Rossmann-fold core β-sheet.
+) The class I-characterizing <scene name='Sandbox_Reserved_704/Domain_1/2'>Rossmann-fold aminoacylation catalytic domain</scene>: It contains the HIGH motif. It is located at the beginning of the long α-helix found below the Rossmann-fold core β-sheet.
 Other the Rossmann fold domain, there are other fused and inserted domains:
@@ Line 33: / Line 33: @@
 ) The <scene name='Sandbox_Reserved_704/Lsd1/1'>LSD (Leucine-specific domain) 1</scene> and 8) <scene name='Sandbox_Reserved_704/Domain_8/1'>LSD2</scene> 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/Domain_9/1'>SC-fold domain</scene>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>.
+) The <scene name='Sandbox_Reserved_704/Domain_9/1'>SC-fold domain</scene> 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>.