Dihydrolipoamide acetyltransferase

From Proteopedia

Revision as of 11:50, 7 March 2013

Template:STRUCTURE 1b5s 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

Updated on 07-March-2013

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