Sandbox Reserved 346: Difference between revisions

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=='''Structure'''==

<scene name='Sandbox_Reserved_346/Ast/1'>AST</scene> is a homodimer that contains 16 alpha helices and a Beta-sheet formed from 7 parallel and antiparallel strands. Each subunit contains an equivalent active site<ref name ="AST Structure">PMID:2121725</ref>. The subunits connect at two sites: between their large domains and between the N-terminal residues and the large domain on the other subunit. This structure of AST varies minutely among organisms ranging from ''E. coli'' to humans. As well, the structure of the active site is highly conserved with a sequence homology of 25%.

<scene name='Sandbox_Reserved_346/Ast/1'>AST</scene> is a homodimer that contains 16 alpha helices and a Beta-sheet formed from 7 parallel and antiparallel strands<ref name ="AST Structure"/>. Each subunit contains an equivalent active site<ref name ="AST Structure">PMID:2121725</ref>. The subunits connect at two sites: between their large domains and between the N-terminal residues and the large domain on the other subunit<ref name ="AST Structure"/>. This structure of AST varies minutely among organisms ranging from ''E. coli'' to humans<ref name ="AST Structure"/><ref name ="AST ROLES AND STRUCTURE"/>. As well, the structure of the active site is highly conserved with a sequence homology of 25%<ref name ="AST Structure"/>.

Each subunit of the homodimer is further divided into a small and large domain. The <scene name='Sandbox_Reserved_346/Small_subunit_2/1'>small domain</scene> is comprised of the amino acids from the N-terminus to Pro 48 residue and from Met 326 to the C-terminus. The remaining amino acids make up the <scene name='Sandbox_Reserved_346/Large_subunit/1'>large domain</scene>, and the <scene name='Sandbox_Reserved_346/Whole_subunit_2/1'>two domains</scene> are connected by a long alpha helicx consisting of 32 amino acids<ref name ="AST Structure"/>.

Each subunit of the homodimer is further divided into a small and large domain<ref name ="AST Structure"/>. The <scene name='Sandbox_Reserved_346/Small_subunit_2/1'>small domain</scene> is comprised of the amino acids from the N-terminus to Pro 48 residue and from Met 326 to the C-terminus<ref name ="AST Structure"/>. The remaining amino acids make up the <scene name='Sandbox_Reserved_346/Large_subunit/1'>large domain</scene>, and the <scene name='Sandbox_Reserved_346/Whole_subunit_2/1'>two domains</scene> are connected by a long alpha helicx consisting of 32 amino acids<ref name ="AST Structure"/>.

The large domain is where the active site of AST is found and to accommodate this, the core contains many alpha/beta supersecondary structures. This is contrasted with the core of the small subunit which is formed from two alpha helices and two beta strands. In multicellular organisms there is a kink at the 325th residue which acts as a hinge for the small domain, which allows for the resulting conformational changes that take place upon the binding of inhibitors to the enzyme.

The large domain is where the active site of AST is found and to accommodate this, the core contains many alpha/beta supersecondary structures<ref name ="AST Structure"/>. This is contrasted with the core of the small subunit which is formed from two alpha helices and two beta strands<ref name ="AST Structure"/>. In multicellular organisms there is a kink at the 325th residue which acts as a hinge for the small domain, which allows for the resulting conformational changes that take place upon the binding of inhibitors to the enzyme<ref name ="AST Structure"/>.

As was stated above, the active site of AST is situated on the large domain of the subunit. Within the active site is the amino residue Lys 258, also known as the internal aldimine, which binds with the cofactor Pyridoxal 5'-phosphate (<scene name='Sandbox_Reserved_346/Plp/5'>PLP</scene>) forming what is called a [http://en.wikipedia.org/wiki/Schiff_base Schiff base]. Upon the addition of an amino acid substrate, a new Schiiff base forms between PLP and the amino acid

As was stated above, the active site of AST is situated on the large domain of the subunit<ref name ="AST Structure"/>. Within the active site is the amino residue Lys 258, also known as the internal aldimine, which binds with the cofactor Pyridoxal 5'-phosphate (<scene name='Sandbox_Reserved_346/Plp/5'>PLP</scene>) forming what is called a [http://en.wikipedia.org/wiki/Schiff_base Schiff base]<ref name ="AST Structure"/><ref name ="AST ROLES AND STRUCTURE"/>. Upon the addition of an amino acid substrate, a new Schiiff base forms between PLP and the amino acid<ref name ="AST Structure"/>.

Sandbox Reserved 346: Difference between revisions

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@@ Line 12: / Line 12: @@
 =='''Structure'''==
 <Structure load='1b4x' size='300' frame='true' align='left' caption='Ligand' scene='Sandbox_Reserved_346/Ast/1'/>
-<scene name='Sandbox_Reserved_346/Ast/1'>AST</scene> is a homodimer that contains 16 alpha helices and a Beta-sheet formed from 7 parallel and antiparallel strands. Each subunit contains an equivalent active site<ref name ="AST Structure">PMID:2121725</ref>. The subunits connect at two sites: between their large domains and between the N-terminal residues and the large domain on the other subunit. This structure of AST varies minutely among organisms ranging from ''E. coli'' to humans. As well, the structure of the active site is highly conserved with a sequence homology of 25%.
+<scene name='Sandbox_Reserved_346/Ast/1'>AST</scene> is a homodimer that contains 16 alpha helices and a Beta-sheet formed from 7 parallel and antiparallel strands<ref name ="AST Structure"/>. Each subunit contains an equivalent active site<ref name ="AST Structure">PMID:2121725</ref>. The subunits connect at two sites: between their large domains and between the N-terminal residues and the large domain on the other subunit<ref name ="AST Structure"/>. This structure of AST varies minutely among organisms ranging from ''E. coli'' to humans<ref name ="AST Structure"/><ref name ="AST ROLES AND STRUCTURE"/>. As well, the structure of the active site is highly conserved with a sequence homology of 25%<ref name ="AST Structure"/>.
-Each subunit of the homodimer is further divided into a small and large domain. The <scene name='Sandbox_Reserved_346/Small_subunit_2/1'>small domain</scene> is comprised of the amino acids from the N-terminus to Pro 48 residue and from Met 326  to the C-terminus. The remaining amino acids make up the <scene name='Sandbox_Reserved_346/Large_subunit/1'>large domain</scene>, and the <scene name='Sandbox_Reserved_346/Whole_subunit_2/1'>two domains</scene> are connected by a long alpha helicx consisting of 32 amino acids<ref name ="AST Structure"/>.
+Each subunit of the homodimer is further divided into a small and large domain<ref name ="AST Structure"/>. The <scene name='Sandbox_Reserved_346/Small_subunit_2/1'>small domain</scene> is comprised of the amino acids from the N-terminus to Pro 48 residue and from Met 326  to the C-terminus<ref name ="AST Structure"/>. The remaining amino acids make up the <scene name='Sandbox_Reserved_346/Large_subunit/1'>large domain</scene>, and the <scene name='Sandbox_Reserved_346/Whole_subunit_2/1'>two domains</scene> are connected by a long alpha helicx consisting of 32 amino acids<ref name ="AST Structure"/>.
-The large domain is where the active site of AST is found and to accommodate this, the core contains many alpha/beta supersecondary structures. This is contrasted with the core of the small subunit which is formed from two alpha helices and two beta strands. In multicellular organisms there is a kink at the 325th residue which acts as a hinge for the small domain, which allows for the resulting conformational changes that take place upon the binding of inhibitors to the enzyme.
+The large domain is where the active site of AST is found and to accommodate this, the core contains many alpha/beta supersecondary structures<ref name ="AST Structure"/>. This is contrasted with the core of the small subunit which is formed from two alpha helices and two beta strands<ref name ="AST Structure"/>. In multicellular organisms there is a kink at the 325th residue which acts as a hinge for the small domain, which allows for the resulting conformational changes that take place upon the binding of inhibitors to the enzyme<ref name ="AST Structure"/>.
-As was stated above, the active site of AST is situated on the large domain of the subunit. Within the active site is the amino residue Lys 258, also known as the internal aldimine, which binds with the cofactor Pyridoxal 5'-phosphate (<scene name='Sandbox_Reserved_346/Plp/5'>PLP</scene>) forming what is called a [http://en.wikipedia.org/wiki/Schiff_base Schiff base]. Upon the addition of an amino acid substrate, a new Schiiff base forms between PLP and the amino acid
+As was stated above, the active site of AST is situated on the large domain of the subunit<ref name ="AST Structure"/>. Within the active site is the amino residue Lys 258, also known as the internal aldimine, which binds with the cofactor Pyridoxal 5'-phosphate (<scene name='Sandbox_Reserved_346/Plp/5'>PLP</scene>) forming what is called a [http://en.wikipedia.org/wiki/Schiff_base Schiff base]<ref name ="AST Structure"/><ref name ="AST ROLES AND STRUCTURE"/>. Upon the addition of an amino acid substrate, a new Schiiff base forms between PLP and the amino acid<ref name ="AST Structure"/>.