Aspartate Aminotransferase

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<StructureSection load='1asn' size='400' side='right' scene='' caption=''>
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{{STRUCTURE_1asn|PDB=1asn|SCENE= | CAPTION=Aspartate aminotransferase dimer complex with sulfate and pyridoxal phosphate, [[1asn]]}}
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='''Aspartate Aminotransferase'''=
='''Aspartate Aminotransferase'''=
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__TOC__
__TOC__
=='''Structure'''==
=='''Structure'''==
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<Structure load='1b4x' size='300' frame='true' align='left' caption='Figure 1: Asymetric unit of Aspartate aminotransferase, with highlighted small and large domain and PLP cofactor, [[1b4x]]' scene='Sandbox_Reserved_346/Ast/1'/>
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<scene name='Sandbox_Reserved_346/Ast/1'>AST</scene> is a homodimer that contains 16 α-helices and a β-sheet formed from 7 parallel and antiparallel strands <ref name ="AST Structure"/>. Asymetric 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<ref name ="AAT 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"/>.
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<scene name='Sandbox_Reserved_346/Ast/1'>AST</scene> is a homodimer that contains 16 α-helices and a β-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 ="AAT 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"/>.
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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"/>.
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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"/>.
The large domain is where the active site of AAT is found and to accommodate this, the core contains many α/β supersecondary structures<ref name ="AST Structure"/>. This is contrasted with the core of the small subunit which is formed from two α-helices and two β-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"/>.
The large domain is where the active site of AAT is found and to accommodate this, the core contains many α/β supersecondary structures<ref name ="AST Structure"/>. This is contrasted with the core of the small subunit which is formed from two α-helices and two β-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"/>.

Revision as of 13:23, 24 November 2014

PDB ID 1asn

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Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Luke Spooner

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