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| | <StructureSection load='6zzj' size='340' side='right'caption='[[6zzj]], [[Resolution|resolution]] 1.35Å' scene=''> | | <StructureSection load='6zzj' size='340' side='right'caption='[[6zzj]], [[Resolution|resolution]] 1.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6zzj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Corgl Corgl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZZJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZZJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6zzj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_glutamicum_ATCC_13032 Corynebacterium glutamicum ATCC 13032]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZZJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZZJ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAO:OXIDIZED+COENZYME+A'>CAO</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.35Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aceF, sucB, Cgl2207, cg2421 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=196627 CORGL])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAO:OXIDIZED+COENZYME+A'>CAO</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_acetyltransferase Dihydrolipoyllysine-residue acetyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.12 2.3.1.12] </span></td></tr>
| + | |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6zzj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zzj OCA], [https://pdbe.org/6zzj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zzj RCSB], [https://www.ebi.ac.uk/pdbsum/6zzj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zzj ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6zzj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zzj OCA], [https://pdbe.org/6zzj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zzj RCSB], [https://www.ebi.ac.uk/pdbsum/6zzj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zzj ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/ODP2_CORGL ODP2_CORGL]] Is essential for both 2-oxoglutarate dehydrogenase (ODH) and pyruvate dehydrogenase (PDH) activities, but AceF has exclusively transacetylase (and no transsuccinylase) activity. The lipoyl residues required for ODH activity are likely provided by AceF.<ref>PMID:20675489</ref>
| + | [https://www.uniprot.org/uniprot/ODP2_CORGL ODP2_CORGL] Is essential for both 2-oxoglutarate dehydrogenase (ODH) and pyruvate dehydrogenase (PDH) activities, but AceF has exclusively transacetylase (and no transsuccinylase) activity. The lipoyl residues required for ODH activity are likely provided by AceF.<ref>PMID:20675489</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6zzj" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6zzj" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Dihydrolipoamide acetyltransferase 3D structures|Dihydrolipoamide acetyltransferase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Corgl]] | + | [[Category: Corynebacterium glutamicum ATCC 13032]] |
| - | [[Category: Dihydrolipoyllysine-residue acetyltransferase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bellinzoni, M]] | + | [[Category: Bellinzoni M]] |
| - | [[Category: Bruch, E M]] | + | [[Category: Bruch EM]] |
| - | [[Category: Lexa-Sapart, N]] | + | [[Category: Lexa-Sapart N]] |
| - | [[Category: Acetyltransferase]]
| + | |
| - | [[Category: Coa]]
| + | |
| - | [[Category: Corynebacterium]]
| + | |
| - | [[Category: Lipoamide]]
| + | |
| - | [[Category: Odh]]
| + | |
| - | [[Category: Pdh]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
ODP2_CORGL Is essential for both 2-oxoglutarate dehydrogenase (ODH) and pyruvate dehydrogenase (PDH) activities, but AceF has exclusively transacetylase (and no transsuccinylase) activity. The lipoyl residues required for ODH activity are likely provided by AceF.[1]
Publication Abstract from PubMed
alpha-oxoacid dehydrogenase complexes are large, tripartite enzymatic machineries carrying out key reactions in central metabolism. Extremely conserved across the tree of life, they have been, so far, all considered to be structured around a high-molecular weight hollow core, consisting of up to 60 subunits of the acyltransferase component. We provide here evidence that Actinobacteria break the rule by possessing an acetyltranferase component reduced to its minimally active, trimeric unit, characterized by a unique C-terminal helix bearing an actinobacterial specific insertion that precludes larger protein oligomerization. This particular feature, together with the presence of an odhA gene coding for both the decarboxylase and the acyltransferase domains on the same polypetide, is spread over Actinobacteria and reflects the association of PDH and ODH into a single physical complex. Considering the central role of the pyruvate and 2-oxoglutarate nodes in central metabolism, our findings pave the way to both therapeutic and metabolic engineering applications.
Actinobacteria challenge the paradigm: A unique protein architecture for a well-known, central metabolic complex.,Bruch EM, Vilela P, Yang L, Boyko A, Lexa-Sapart N, Raynal B, Alzari PM, Bellinzoni M Proc Natl Acad Sci U S A. 2021 Nov 30;118(48). pii: 2112107118. doi:, 10.1073/pnas.2112107118. PMID:34819376[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hoffelder M, Raasch K, van Ooyen J, Eggeling L. The E2 domain of OdhA of Corynebacterium glutamicum has succinyltransferase activity dependent on lipoyl residues of the acetyltransferase AceF. J Bacteriol. 2010 Oct;192(19):5203-11. doi: 10.1128/JB.00597-10. Epub 2010 Jul, 30. PMID:20675489 doi:http://dx.doi.org/10.1128/JB.00597-10
- ↑ Bruch EM, Vilela P, Yang L, Boyko A, Lexa-Sapart N, Raynal B, Alzari PM, Bellinzoni M. Actinobacteria challenge the paradigm: A unique protein architecture for a well-known, central metabolic complex. Proc Natl Acad Sci U S A. 2021 Nov 30;118(48). pii: 2112107118. doi:, 10.1073/pnas.2112107118. PMID:34819376 doi:http://dx.doi.org/10.1073/pnas.2112107118
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