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| | <StructureSection load='6zzn' size='340' side='right'caption='[[6zzn]], [[Resolution|resolution]] 1.50Å' scene=''> | | <StructureSection load='6zzn' size='340' side='right'caption='[[6zzn]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6zzn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZZN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZZN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6zzn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZZN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZZN FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</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]] 1.5Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bkdC, pdhC, Rv2495c ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</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_(2-methylpropanoyl)transferase Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.168 2.3.1.168] </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=6zzn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zzn OCA], [https://pdbe.org/6zzn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zzn RCSB], [https://www.ebi.ac.uk/pdbsum/6zzn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zzn 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=6zzn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zzn OCA], [https://pdbe.org/6zzn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zzn RCSB], [https://www.ebi.ac.uk/pdbsum/6zzn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zzn ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/BKDC_MYCTU BKDC_MYCTU]] Component of the branched-chain alpha-ketoacid dehydrogenase (BCKADH) complex, that catalyzes the overall conversion of branched-chain alpha-ketoacids to acyl-CoA and CO(2).<ref>PMID:21238944</ref>
| + | [https://www.uniprot.org/uniprot/BKDC_MYCTU BKDC_MYCTU] Component of the branched-chain alpha-ketoacid dehydrogenase (BCKADH) complex, that catalyzes the overall conversion of branched-chain alpha-ketoacids to acyl-CoA and CO(2).<ref>PMID:21238944</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Myctu]] | + | [[Category: Mycobacterium tuberculosis H37Rv]] |
| - | [[Category: Bellinzoni, M]] | + | [[Category: Bellinzoni M]] |
| - | [[Category: Vilela, P]] | + | [[Category: Vilela P]] |
| - | [[Category: Acyltransferase]]
| + | |
| - | [[Category: Bckdh]]
| + | |
| - | [[Category: Coa]]
| + | |
| - | [[Category: Lipoamide]]
| + | |
| - | [[Category: Mycobacterium]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Tuberculosis]]
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| Structural highlights
Function
BKDC_MYCTU Component of the branched-chain alpha-ketoacid dehydrogenase (BCKADH) complex, that catalyzes the overall conversion of branched-chain alpha-ketoacids to acyl-CoA and CO(2).[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.
References
- ↑ Venugopal A, Bryk R, Shi S, Rhee K, Rath P, Schnappinger D, Ehrt S, Nathan C. Virulence of Mycobacterium tuberculosis depends on lipoamide dehydrogenase, a member of three multienzyme complexes. Cell Host Microbe. 2011 Jan 20;9(1):21-31. doi: 10.1016/j.chom.2010.12.004. PMID:21238944 doi:http://dx.doi.org/10.1016/j.chom.2010.12.004
- ↑ 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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