Sandbox Reserved 704: Difference between revisions

Line 23:

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

2) <scene name='Sandbox_Reserved_704/Domain_2/1'>CP (Connective Peptide)-core</scene> and 3)<scene name='Sandbox_Reserved_704/Domain_3/2'>CP1 hairpin</scene> consist of antiparallel β-sheets, but only the CP-core is fixed on the aminoacylation domain. There is a “joint” formed by the junction of the CP-core and the CP1 hairpin (Ala180 and His462 residues) which is essential for accommodating the tRNA <ref name="">PMID:16155584</ref>.

2) The <scene name='Sandbox_Reserved_704/Domain_2/1'>CP (Connective Peptide)-core</scene> and 3) The <scene name='Sandbox_Reserved_704/Domain_3/2'>CP1 hairpin</scene> consist of antiparallel β-sheets, but only the CP-core is fixed on the aminoacylation domain. There is a “joint” formed by the junction of the CP-core and the CP1 hairpin (Ala180 and His462 residues) which is essential for accommodating the tRNA <ref name="">PMID:16155584</ref>.

4) <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 residue Asp 332 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 residue Asp 332 is necessary for post-transfer editing <ref name="Fukunaga">PMID:15663927</ref>.

5) CP2 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.

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.

Sandbox Reserved 704: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 23: / Line 23: @@
 Other the Rossmann fold domain, there are other fused and inserted domains:
-) <scene name='Sandbox_Reserved_704/Domain_2/1'>CP (Connective Peptide)-core</scene> and 3)<scene name='Sandbox_Reserved_704/Domain_3/2'>CP1 hairpin</scene> consist of antiparallel β-sheets, but only the CP-core is fixed on the aminoacylation domain. There is a “joint” formed by the junction of the CP-core and the CP1 hairpin (Ala180 and His462 residues) which is essential for accommodating the tRNA <ref name="">PMID:16155584</ref>.
+) The <scene name='Sandbox_Reserved_704/Domain_2/1'>CP (Connective Peptide)-core</scene> and 3) The <scene name='Sandbox_Reserved_704/Domain_3/2'>CP1 hairpin</scene> consist of antiparallel β-sheets, but only the CP-core is fixed on the aminoacylation domain. There is a “joint” formed by the junction of the CP-core and the CP1 hairpin (Ala180 and His462 residues) which is essential for accommodating the tRNA <ref name="">PMID:16155584</ref>.
-) <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 residue Asp 332 is necessary for post-transfer editing <ref name="Fukunaga">PMID:15663927</ref>.
+) 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 residue Asp 332 is necessary for post-transfer editing <ref name="Fukunaga">PMID:15663927</ref>.
-) CP2 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.
+) 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.