6zzi: Difference between revisions
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==Crystal structure of the catalyic domain of Corynebacterium glutamicum acetyltransferase AceF (E2p).== | |||
<StructureSection load='6zzi' size='340' side='right'caption='[[6zzi]], [[Resolution|resolution]] 1.93Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6zzi]] is a 6 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=6ZZI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZZI FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.932Å</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=6zzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zzi OCA], [https://pdbe.org/6zzi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zzi RCSB], [https://www.ebi.ac.uk/pdbsum/6zzi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zzi ProSAT]</span></td></tr> | |||
</table> | |||
== 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> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:34819376</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Bellinzoni | <div class="pdbe-citations 6zzi" style="background-color:#fffaf0;"></div> | ||
[[Category: Bruch | |||
[[Category: Lexa-Sapart | ==See Also== | ||
*[[Dihydrolipoamide acetyltransferase 3D structures|Dihydrolipoamide acetyltransferase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Corynebacterium glutamicum ATCC 13032]] | |||
[[Category: Large Structures]] | |||
[[Category: Bellinzoni M]] | |||
[[Category: Bruch EM]] | |||
[[Category: Lexa-Sapart N]] | |||
Latest revision as of 15:00, 1 February 2024
Crystal structure of the catalyic domain of Corynebacterium glutamicum acetyltransferase AceF (E2p).Crystal structure of the catalyic domain of Corynebacterium glutamicum acetyltransferase AceF (E2p).
Structural highlights
FunctionODP2_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 PubMedalpha-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 AlsoReferences
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