Sandbox Reserved 704: Difference between revisions
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4) The <scene name='Sandbox_Reserved_704/Domain_4/1'>CP1 editing domain</scene> is located in the middle of the CP1 hairpin. It is the editing domain, that means that this region is responsible for the hydrolysis of the incorrectly synthesized products. Because LeuRS have a specific editing activity that hydrolyzes misactivated aminoacyl-adenylates (pre-transfer editing) and mischarged aminoacyl-tRNAs (post-transfer editing) or both when they have misformed with noncognate amino acids.The <scene name='Sandbox_Reserved_704/Asp332/1'>residue Asp 332</scene> is necessary for post-transfer editing <ref name="Fukunaga">PMID:15663927</ref>. | 4) The <scene name='Sandbox_Reserved_704/Domain_4/1'>CP1 editing domain</scene> is located in the middle of the CP1 hairpin. It is the editing domain, that means that this region is responsible for the hydrolysis of the incorrectly synthesized products. Because LeuRS have a specific editing activity that hydrolyzes misactivated aminoacyl-adenylates (pre-transfer editing) and mischarged aminoacyl-tRNAs (post-transfer editing) or both when they have misformed with noncognate amino acids.The <scene name='Sandbox_Reserved_704/Asp332/1'>residue Asp 332</scene> is necessary for post-transfer editing <ref name="Fukunaga">PMID:15663927</ref>. | ||
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 | 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. This domain is necessary for the amino acid activation and post-transfer editing <ref name="Zhou XL,Zhu B">PMID:18955487</ref>. | ||
6) The <scene name='Sandbox_Reserved_704/Lsd1/1'>LSD (Leucine-specific domain) 1</scene> and 7) <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>. | 6) The <scene name='Sandbox_Reserved_704/Lsd1/1'>LSD (Leucine-specific domain) 1</scene> and 7) <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>. | ||
