Dihydrolipoamide acetyltransferase

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<StructureSection load='3duf' size='350' side='right' caption='Dihydrolipoamide acetyltransferase (wheat, blue) complex with E1 subunit α (grey, pink, magenta, gold) and subunit β (green, yellow, cyan, red) (PDB entry [[3duf]])' scene='48/485632/Cv/1'>
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<StructureSection load='' size='350' side='right' caption='Human dihydrolipoamide acetyltransferase binding domain (cyan, green) complex with E3 binding domain (magenta), FAD, CHES and mercaptodthanol (PDB entry [[3rnm]])' scene='48/485632/Cv/3'>
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'''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.<ref>PMID:14736882</ref>
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'''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.<ref>PMID:14736882</ref>
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== Structural highlights ==
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<scene name='48/485632/Cv/9'>Human dihydrolipoamide acetyltransferase binding domain with E3 binding domain, FAD, CHES and mercaptodthanol</scene>.
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<scene name='48/485632/Cv/2'>DLAT</scene>. The DLAT structure contains 3 lipoyl domains, a binding domain and a catalytic domain.
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<scene name='48/485632/Cv/10'>FAD binding site</scene>.
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<scene name='48/485632/Cv/11'>Mercaptodthanol binding site</scene>.
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<scene name='48/485632/Cv/12'>CHES binding site</scene> (PDB entry [[3rnm]]), water molecules shown as red spheres.
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</StructureSection>
</StructureSection>
==3D structures of dihydrolipoamide acetyltransferase==
==3D structures of dihydrolipoamide acetyltransferase==
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[[Dihydrolipoamide acetyltransferase 3D structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
 
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{{#tree:id=OrganizedByTopic|openlevels=0|
 
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*DLAT lipoyl domain
 
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**[[1lab]], [[1lac]] – GsDLAT lipoyl domain – ''Geobacillus stearothermophilus'' – NMR<BR />
 
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**[[1iyu]], [[1iyv]] - DLAT lipoyl domain – ''Azotobacter vinelandii'' – NMR<BR />
 
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**[[1fyc]] - DLAT lipoyl domain – human – NMR<BR />
 
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**[[1qjo]] - EcDLAT lipoyl domain – ''Escherichia coli'' – NMR<BR />
 
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*DLAT binding domain
 
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**[[2pdd]], [[2pde]] – GsDLAT binding domain – NMR<BR />
 
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**[[1w4e]], [[1w4f]], [[1w4g]] - GsDLAT binding domain (mutant) – NMR<BR />
 
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**[[1w4h]] - EcDLAT binding domain – NMR<BR />
 
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**[[1w4i]] - PaDLAT binding domain – ''Pyrobaculum aerophilum'' – NMR<BR />
 
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**[[1w4j]], [[1w4k]] - PaDLAT binding domain (mutant) – NMR<BR />
 
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**[[1ebd]], [[2eq8]], [[2eq9]] - GsDLAT binding domain + E3<BR />
 
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**[[3rnm]] - hDLAT binding domain (mutant) + E3<BR />
 
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**[[1w85]], [[1w88]] - GsDLAT binding domain + E1<br />
 
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**[[1y8n]], [[1y8o]], [[1y8p]] - hDLAT binding domain + pyruvate dehydrogenase kinase
 
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*DLAT catalytic domain
 
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**[[1b5s]] - GsDLAT catalytic domain
 
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**[[2k7v]] – GsDLAT residues 206-293 – NMR<BR />
 
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*Full DLAT
 
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**[[3duf]], [[3dv0]], [[3dva]] - GsDLAT + E1
 
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}}
 
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Human dihydrolipoamide acetyltransferase binding domain (cyan, green) complex with E3 binding domain (magenta), FAD, CHES and mercaptodthanol (PDB entry 3rnm)

Drag the structure with the mouse to rotate

3D structures of dihydrolipoamide acetyltransferase

Dihydrolipoamide acetyltransferase 3D structures

References

  1. ↑ Lai WL, Chou LY, Ting CY, Kirby R, Tsai YC, Wang AH, Liaw SH. The functional role of the binuclear metal center in D-aminoacylase: one-metal activation and second-metal attenuation. J Biol Chem. 2004 Apr 2;279(14):13962-7. Epub 2004 Jan 21. PMID:14736882 doi:http://dx.doi.org/10.1074/jbc.M308849200

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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