Aspartate Aminotransferase: Difference between revisions
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=='''Structure'''== | =='''Structure'''== | ||
<scene name='49/490061/Cv/1'>AST is a homodimer</scene> that contains <scene name='49/490061/Cv/3'>16 α-helices and a β-sheet formed from 7 parallel and antiparallel strands</scene> <ref name ="AST Structure"/> ({{Template:ColorKey_Helix}}, | <scene name='49/490061/Cv/1'>AST is a homodimer</scene> that contains <scene name='49/490061/Cv/3'>16 α-helices and a β-sheet formed from 7 parallel and antiparallel strands</scene> <ref name ="AST Structure"/> ({{Template:ColorKey_Helix}}, | ||
{{Template:ColorKey_Strand}}, {{Template:ColorKey_Loop}}, {{Template:ColorKey_Turn}}). Asymmetric unit of Aspartate aminotransferase, with highlighted small and large domain and PLP cofactor ([[1b4x]]). 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 | {{Template:ColorKey_Strand}}, {{Template:ColorKey_Loop}}, {{Template:ColorKey_Turn}}). Asymmetric unit of Aspartate aminotransferase, with highlighted small and large domain and PLP cofactor ([[1b4x]]). 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<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<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 α-helix 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 α-helix consisting of 32 amino acids<ref name ="AST Structure"/>. | ||