6zzi - Revision history

OCA at 12:00, 1 February 2024

2024-02-01T12:00:51Z

←Older revision		Revision as of 12:00, 1 February 2024
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	<StructureSection load='6zzi' size='340' side='right'caption='[[6zzi]], [[Resolution\|resolution]] 1.93Å' scene=''>		<StructureSection load='6zzi' size='340' side='right'caption='[[6zzi]], [[Resolution\|resolution]] 1.93Å' scene=''>
	== Structural highlights ==		== 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]] 1.932Å</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>		<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>		</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 6zzi" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 6zzi" 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~~]]	+

OCA at 16:54, 15 December 2021

2021-12-15T16:54:03Z

←Older revision		Revision as of 16:54, 15 December 2021
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-	==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]] 1.93Å' scene=''>		<StructureSection load='6zzi' size='340' side='right'caption='[[6zzi]], [[Resolution\|resolution]] 1.93Å' scene=''>
	== Structural highlights ==		== Structural highlights ==

OCA at 10:02, 8 December 2021

2021-12-08T10:02:05Z

←Older revision		Revision as of 10:02, 8 December 2021
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	==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]]' scene=''>	+	<StructureSection load='6zzi' size='340' side='right'caption='[[6zzi]], [[Resolution\|resolution]] 1.93Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>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/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>
-	</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>	+	</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='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>		</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>
		+	</div>
		+	<div class="pdbe-citations 6zzi" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Corgl]]
		+	[[Category: Dihydrolipoyllysine-residue acetyltransferase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Bellinzoni M]]	+	[[Category: Bellinzoni, M]]
-	[[Category: Bruch EM]]	+	[[Category: Bruch, E M]]
-	[[Category: Lexa-Sapart N]]	+	[[Category: Lexa-Sapart, N]]
		+	[[Category: Acetyltransferase]]
		+	[[Category: Coa]]
		+	[[Category: Corynebacterium]]
		+	[[Category: Lipoamide]]
		+	[[Category: Odh]]
		+	[[Category: Pdh]]
		+	[[Category: Transferase]]

OCA at 06:06, 18 August 2021

2021-08-18T06:06:17Z

←Older revision		Revision as of 06:06, 18 August 2021
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6zzi ~~is ON HOLD until Paper Publication~~	+	==Crystal structure of the catalyic domain of Corynebacterium glutamicum acetyltransferase AceF (E2p)==
-		+	<StructureSection load='6zzi' size='340' side='right'caption='[[6zzi]]' scene=''>
-	~~Authors~~: ~~Bruch, E~~.M., ~~Lexa~~-~~Sapart~~, N., ~~Bellinzoni~~, M.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>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>
-	~~Description: Crystal structure of the catalyic domain of Corynebacterium glutamicum acetyltransferase AceF (E2p)~~	+	</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>
-	[[Category: ~~Unreleased~~ Structures]]	+	</table>
-	[[Category: Bellinzoni, M]]	+	__TOC__
-	[[Category: Bruch~~, E.M~~]]	+	</StructureSection>
-	[[Category: Lexa-Sapart, N]]	+	[[Category: Large Structures]]
		+	[[Category: Bellinzoni M]]
		+	[[Category: Bruch EM]]
		+	[[Category: Lexa-Sapart N]]

OCA at 05:00, 2 September 2020

2020-09-02T05:00:17Z

←Older revision		Revision as of 05:00, 2 September 2020
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6zzi is ON HOLD	+	The entry 6zzi is ON HOLD until Paper Publication

	Authors: Bruch, E.M., Lexa-Sapart, N., Bellinzoni, M.		Authors: Bruch, E.M., Lexa-Sapart, N., Bellinzoni, M.

-	Description: Crystal structure of the ~~cataltyic~~ domain of Corynebacterium glutamicum acetyltransferase AceF (E2p)	+	Description: Crystal structure of the catalyic domain of Corynebacterium glutamicum acetyltransferase AceF (E2p)
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
		+	[[Category: Bellinzoni, M]]
	[[Category: Bruch, E.M]]		[[Category: Bruch, E.M]]
	[[Category: Lexa-Sapart, N]]		[[Category: Lexa-Sapart, N]]
-	[[Category: Bellinzoni, M]]

OCA: Protected "6zzi" [edit=sysop:move=sysop]

2020-08-12T08:17:06Z

Protected "6zzi" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:17, 12 August 2020

OCA: New page: '''Unreleased structure''' The entry 6zzi is ON HOLD Authors: Bruch, E.M., Lexa-Sapart, N., Bellinzoni, M. Description: Crystal structure of the cataltyic domain of Corynebacterium glu...

2020-08-12T08:17:05Z

New page: '''Unreleased structure''' The entry 6zzi is ON HOLD Authors: Bruch, E.M., Lexa-Sapart, N., Bellinzoni, M. Description: Crystal structure of the cataltyic domain of Corynebacterium glu...

New page

'''Unreleased structure'''

The entry 6zzi is ON HOLD

Authors: Bruch, E.M., Lexa-Sapart, N., Bellinzoni, M.

Description: Crystal structure of the cataltyic domain of Corynebacterium glutamicum acetyltransferase AceF (E2p)
[[Category: Unreleased Structures]]
[[Category: Bruch, E.M]]
[[Category: Lexa-Sapart, N]]
[[Category: Bellinzoni, M]]