Dihydrolipoamide acetyltransferase
From Proteopedia
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| - | {{STRUCTURE_3duf| PDB=3duf | SIZE=400| SCENE= |right|CAPTION=Dihydrolipoamide acetyltransferase complex with pyruvate dehydrogenase [[3duf]] }} | + | {{STRUCTURE_3duf| PDB=3duf | SIZE=400| SCENE= |right|CAPTION=Dihydrolipoamide acetyltransferase complex with pyruvate dehydrogenase, hydroxymethyl-deaza-trihydrogen diphosphate and Mg+2 ion [[3duf]] }} |
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Revision as of 13:21, 13 March 2012
Template:STRUCTURE 3duf Dihydrolipoamide acetyltransferase (DLAT) or E2 is part of the pyruvate dehydrogenase complex together with pyruvate dehydrogenase (E1) and dihydrolipoyl dehydrogenase (E3). The complex decarboxylates pyruvate thus linking the glycolysis to the citric acid cycle. DLAT catalyzes the transfer of acetyl group to CoA. The DLAT structure contains 3 lipoyl domains, a binding domain and a catalytic domain.
3D structures of dihydrolipoamide acetyltransferase
DLAT lipoyl domain
1lab, 1lac – GsDLAT lipoyl domain – Geobacillus stearothermophilus – NMR
1iyu, 1iyv - DLAT lipoyl domain – Azotobacter vinelandii – NMR
1fyc - DLAT lipoyl domain – human – NMR
1qjo - EcDLAT lipoyl domain – Escherichia coli – NMR
DLAT binding domain
2pdd, 2pde – GsDLAT binding domain – NMR
1w4e, 1w4f, 1w4g - GsDLAT binding domain (mutant) – NMR
1w4h - EcDLAT binding domain – NMR
1w4i - PaDLAT binding domain – Pyrobaculum aerophilum – NMR
1w4j, 1w4k - PaDLAT binding domain (mutant) – NMR
1ebd, 2eq8, 2eq9 - GsDLAT binding domain + E3
3rnm - hDLAT binding domain (mutant) + E3
1w85, 1w88 - GsDLAT binding domain + E1
1y8n, 1y8o, 1y8p - hDLAT binding domain + pyruvate dehydrogenase kinase
DLAT catalytic domain
1b5s - GsDLAT catalytic domain
2k7v – GsDLAT residues 206-293 – NMR
Full DLAT
3duf, 3dv0, 3dva - GsDLAT + E1
