6zzi

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of the catalyic domain of Corynebacterium glutamicum acetyltransferase AceF (E2p).

Structural highlights

6zzi is a 6 chain structure with sequence from Corynebacterium glutamicum ATCC 13032. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.932Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6zzi"

Categories: Corynebacterium glutamicum ATCC 13032 | Large Structures | Bellinzoni M | Bruch EM | Lexa-Sapart N

@@ Line 1: / Line 1: @@
-==Crystal structure of the catalyic domain of Corynebacterium glutamicum acetyltransferase AceF (E2p)==
+==Crystal structure of the catalyic domain of Corynebacterium glutamicum acetyltransferase AceF (E2p).==
 <StructureSection load='6zzi' size='340' side='right'caption='[[6zzi]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6zzi]] is a 6 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=6ZZI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZZI FirstGlance]. <br>
+<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='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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.932&#8491;</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=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>
+[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 ==
@@ Line 19: / Line 18: @@
 </div>
 <div class="pdbe-citations 6zzi" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Dihydrolipoamide acetyltransferase 3D structures|Dihydrolipoamide acetyltransferase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Corgl]]
+[[Category: Corynebacterium glutamicum ATCC 13032]]
-[[Category: Dihydrolipoyllysine-residue acetyltransferase]]
 [[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]]

6zzi

From Proteopedia

Current revision

Crystal structure of the catalyic domain of Corynebacterium glutamicum acetyltransferase AceF (E2p).

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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