5dw5 - Revision history

OCA at 22:02, 28 June 2023

OCA — Wed, 28 Jun 2023 22:02:21 GMT

←Older revision		Revision as of 22:02, 28 June 2023
Line 3:		Line 3:
	<StructureSection load='5dw5' size='340' side='right'caption='[[5dw5]], [[Resolution\|resolution]] 1.66Å' scene=''>		<StructureSection load='5dw5' size='340' side='right'caption='[[5dw5]], [[Resolution\|resolution]] 1.66Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5dw5]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Acetobacter_aceti_1023 Acetobacter aceti 1023]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DW5 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5DW5 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5dw5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acetobacter_aceti_1023 Acetobacter aceti 1023]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DW5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DW5 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0T1:[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl]+[(3R)-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(propylamino)propyl]amino]butyl]+hydrogen+phosphate'>0T1</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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]] 1.656Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4eu5\|4eu5]], [[5ddk\|5ddk]], [[5dw4\|5dw4]], [[5dw6\|5dw6]]</td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0T1:[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl]+[(3R)-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(propylamino)propyl]amino]butyl]+hydrogen+phosphate'>0T1</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">AZ09_02565 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1457393 Acetobacter aceti 1023])</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=5dw5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dw5 OCA], [https://pdbe.org/5dw5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dw5 RCSB], [https://www.ebi.ac.uk/pdbsum/5dw5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dw5 ProSAT]</span></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Succinyl-CoA:acetate_CoA-transferase Succinyl-CoA:acetate CoA-transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.3.18 2.8.3.18] </span></td></tr>	+
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=5dw5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dw5 OCA], [~~http~~://pdbe.org/5dw5 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5dw5 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5dw5 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5dw5 ProSAT]</span></td></tr>	+
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/SCACT_ACEAC SCACT_ACEAC] Utilizes succinyl-CoA to convert toxic acetate to acetyl-CoA and succinate. Required for growth on acetic acid and for resistance to high levels of acetic acid. Has also low activity with acetoacetate as substrate.<ref>PMID:18502856</ref> <ref>PMID:23030530</ref> <ref>PMID:18502856</ref> [REFERENCE:3]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 25:
	[[Category: Acetobacter aceti 1023]]		[[Category: Acetobacter aceti 1023]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Succinyl-CoA:acetate CoA-transferase]]~~	+	[[Category: Kappock TJ]]
-	[[Category: Kappock~~, T J~~]]	+	[[Category: Murphy JR]]
-	[[Category: Murphy~~, J R]]~~	+
-	~~[[Category: Acidophile]]~~	+
-	~~[[Category: Transferase]]~~	+
-	~~[[Category: Tricarboxylic acid cycle~~]]	+

OCA at 08:09, 15 April 2020

OCA — Wed, 15 Apr 2020 08:09:49 GMT

←Older revision		Revision as of 08:09, 15 April 2020
Line 1:		Line 1:

	==Succinyl-CoA:acetate CoA-transferase (AarCH6) bound to the CoA analogue 3'-phosphoadenosine 5'-(O-(N-propylpantothenamide))pyrophosphate (MX)==		==Succinyl-CoA:acetate CoA-transferase (AarCH6) bound to the CoA analogue 3'-phosphoadenosine 5'-(O-(N-propylpantothenamide))pyrophosphate (MX)==
-	<StructureSection load='5dw5' size='340' side='right' caption='[[5dw5]], [[Resolution\|resolution]] 1.66Å' scene=''>	+	<StructureSection load='5dw5' size='340' side='right'caption='[[5dw5]], [[Resolution\|resolution]] 1.66Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5dw5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DW5 OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5DW5 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5dw5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Acetobacter_aceti_1023 Acetobacter aceti 1023]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DW5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5DW5 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0T1:[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl]+[(3R)-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(propylamino)propyl]amino]butyl]+hydrogen+phosphate'>0T1</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0T1:[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl]+[(3R)-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(propylamino)propyl]amino]butyl]+hydrogen+phosphate'>0T1</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4eu5\|4eu5]], [[5ddk\|5ddk]], [[5dw4\|5dw4]], [[5dw6\|5dw6]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4eu5\|4eu5]], [[5ddk\|5ddk]], [[5dw4\|5dw4]], [[5dw6\|5dw6]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">AZ09_02565 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1457393 Acetobacter aceti 1023])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Succinyl-CoA:acetate_CoA-transferase Succinyl-CoA:acetate CoA-transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.3.18 2.8.3.18] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Succinyl-CoA:acetate_CoA-transferase Succinyl-CoA:acetate CoA-transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.3.18 2.8.3.18] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5dw5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dw5 OCA], [http://pdbe.org/5dw5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dw5 RCSB], [http://www.ebi.ac.uk/pdbsum/5dw5 PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5dw5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dw5 OCA], [http://pdbe.org/5dw5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dw5 RCSB], [http://www.ebi.ac.uk/pdbsum/5dw5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dw5 ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 22:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Acetobacter aceti 1023]]
		+	[[Category: Large Structures]]
	[[Category: Succinyl-CoA:acetate CoA-transferase]]		[[Category: Succinyl-CoA:acetate CoA-transferase]]
	[[Category: Kappock, T J]]		[[Category: Kappock, T J]]

OCA at 07:59, 20 June 2016

OCA — Mon, 20 Jun 2016 07:59:22 GMT

←Older revision		Revision as of 07:59, 20 June 2016
Line 11:		Line 11:
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
-	CoA-transferases catalyze ~~transthioesterification reactions involving~~ acyl-CoA ~~substrates, using an active-site carboxylate~~ to ~~form covalent acyl anhydride and CoA-thioester adducts~~. ~~Mechanistic studies of class~~ I CoA-transferases ~~suggested~~ that ~~acyl-~~CoA ~~binding energy is used to accelerate rate-limiting acyl transfers by compressing~~ the ~~substrate thioester tightly against the catalytic glutamate [White~~, H., ~~and Jencks, W. P. (1976) J. Biol. Chem. 251, 1688-1699]. The class I CoA-transferase~~ succinyl-CoA:acetate CoA-transferase ~~is an acetic acid resistance factor~~ (AarC) ~~with a role in a variant citric acid cycle in~~ Acetobacter aceti. ~~In an effort to identify residues involved in substrate recognition, x-ray crystal structures~~ of ~~a C-terminally His(6) tagged form (AarCH6) were determined for several wild-type and~~ mutant ~~complexes, including freeze-trapped acetylglutamyl anhydride and glutamyl~~-CoA ~~thioester adducts. The latter shows~~ the ~~acetate product bound to an auxiliary site~~ that ~~is required for efficient carboxylate substrate recognition. A mutant in which~~ the ~~catalytic~~ glutamate was ~~changed to an alanine~~ crystallized in a closed complex containing ~~dethiaacetyl-CoA~~, ~~which adopts~~ an ~~unusual curled conformation. A model~~ of the ~~acetyl-CoA Michaelis complex demonstrates the compression anticipated four decades ago by Jencks and reveals~~ that ~~the nucleophilic glutamate~~ is ~~held at a~~ near-~~ideal angle for attack as~~ the ~~thioester oxygen is forced into an oxyanion hole composed~~ of ~~Gly388 NH and CoA N2''~~. ~~CoA is nearly immobile along its entire length~~ during ~~all stages of the enzyme reaction~~. ~~Spatial and sequence conservation~~ of ~~key residues indicates~~ that ~~this mechanism is general among class I~~ CoA~~-transferases~~.	+	Coenzyme A (CoA)-transferases catalyze the reversible transfer of CoA from acyl-CoA thioesters to free carboxylates. Class I CoA-transferases produce acylglutamyl anhydride intermediates that undergo attack by CoA thiolate on either the internal or external carbonyl carbon atoms, forming distinct tetrahedral intermediates <3 A apart. In this study, crystal structures of succinyl-CoA:acetate CoA-transferase (AarC) from Acetobacter aceti are used to examine how the Asn347 carboxamide stabilizes the internal oxyanion intermediate. A structure of the active mutant AarC-N347A bound to CoA revealed both solvent replacement of the missing contact and displacement of the adjacent Glu294, indicating that Asn347 both polarizes and orients the essential glutamate. AarC was crystallized with the nonhydrolyzable acetyl-CoA (AcCoA) analog dethiaacetyl-CoA (1a) in an attempt to trap a closed enzyme complex containing a stable analog of the external oxyanion intermediate. One active site contained an acetylglutamyl anhydride adduct and truncated 1a, an unexpected result hinting at an unprecedented cleavage of the ketone moiety in 1a. Solution studies confirmed that 1a decomposition is accompanied by production of near-stoichiometric acetate, in a process that seems to depend on microbial contamination but not AarC. A crystal structure of AarC bound to the postulated 1a truncation product (2a) showed complete closure of one active site per dimer but no acetylglutamyl anhydride, even with acetate added. These findings suggest that an activated acetyl donor forms during 1a decomposition; a working hypothesis involving ketone oxidation is offered. The ability of 2a to induce full active site closure furthermore suggests that it subverts a system used to impede inappropriate active site closure on unacylated CoA.

-	~~Crystal structures~~ of ~~Acetobacter aceti succinyl-coenzyme~~ A (CoA):~~acetate~~ CoA-~~transferase (AarC) reveal specificity determinants and illustrate the mechanism used by class I CoA-transferases~~.,Mullins EA, Kappock TJ ~~Biochemistry~~. ~~2012 Oct 2~~. PMID:~~23030530~~<ref>PMID:~~23030530~~</ref>	+	Functional Dissection of the Bipartite Active Site of the Class I Coenzyme A (CoA)-Transferase Succinyl-CoA:Acetate CoA-Transferase.,Murphy JR, Mullins EA, Kappock TJ Front Chem. 2016 May 23;4:23. doi: 10.3389/fchem.2016.00023. eCollection 2016. PMID:27242998<ref>PMID:27242998</ref>

	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

OCA at 03:37, 11 May 2016

OCA — Wed, 11 May 2016 03:37:30 GMT

←Older revision		Revision as of 03:37, 11 May 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5dw5 is ~~ON HOLD until Paper~~ Publication	+	==Succinyl-CoA:acetate CoA-transferase (AarCH6) bound to the CoA analogue 3'-phosphoadenosine 5'-(O-(N-propylpantothenamide))pyrophosphate (MX)==
		+	<StructureSection load='5dw5' size='340' side='right' caption='[[5dw5]], [[Resolution\|resolution]] 1.66Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5dw5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DW5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DW5 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0T1:[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl]+[(3R)-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(propylamino)propyl]amino]butyl]+hydrogen+phosphate'>0T1</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4eu5\|4eu5]], [[5ddk\|5ddk]], [[5dw4\|5dw4]], [[5dw6\|5dw6]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Succinyl-CoA:acetate_CoA-transferase Succinyl-CoA:acetate CoA-transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.3.18 2.8.3.18] </span></td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5dw5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dw5 OCA], [http://pdbe.org/5dw5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dw5 RCSB], [http://www.ebi.ac.uk/pdbsum/5dw5 PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	CoA-transferases catalyze transthioesterification reactions involving acyl-CoA substrates, using an active-site carboxylate to form covalent acyl anhydride and CoA-thioester adducts. Mechanistic studies of class I CoA-transferases suggested that acyl-CoA binding energy is used to accelerate rate-limiting acyl transfers by compressing the substrate thioester tightly against the catalytic glutamate [White, H., and Jencks, W. P. (1976) J. Biol. Chem. 251, 1688-1699]. The class I CoA-transferase succinyl-CoA:acetate CoA-transferase is an acetic acid resistance factor (AarC) with a role in a variant citric acid cycle in Acetobacter aceti. In an effort to identify residues involved in substrate recognition, x-ray crystal structures of a C-terminally His(6) tagged form (AarCH6) were determined for several wild-type and mutant complexes, including freeze-trapped acetylglutamyl anhydride and glutamyl-CoA thioester adducts. The latter shows the acetate product bound to an auxiliary site that is required for efficient carboxylate substrate recognition. A mutant in which the catalytic glutamate was changed to an alanine crystallized in a closed complex containing dethiaacetyl-CoA, which adopts an unusual curled conformation. A model of the acetyl-CoA Michaelis complex demonstrates the compression anticipated four decades ago by Jencks and reveals that the nucleophilic glutamate is held at a near-ideal angle for attack as the thioester oxygen is forced into an oxyanion hole composed of Gly388 NH and CoA N2''. CoA is nearly immobile along its entire length during all stages of the enzyme reaction. Spatial and sequence conservation of key residues indicates that this mechanism is general among class I CoA-transferases.

-	~~Authors~~: ~~Kappock, T.J~~., ~~Murphy~~, J.R.	+	Crystal structures of Acetobacter aceti succinyl-coenzyme A (CoA):acetate CoA-transferase (AarC) reveal specificity determinants and illustrate the mechanism used by class I CoA-transferases.,Mullins EA, Kappock TJ Biochemistry. 2012 Oct 2. PMID:23030530<ref>PMID:23030530</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
-	[[Category: ~~Murphy~~, J.R]]	+	<div class="pdbe-citations 5dw5" style="background-color:#fffaf0;"></div>
-	[[Category: ~~Kappock~~, T.J]]	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Succinyl-CoA:acetate CoA-transferase]]
		+	[[Category: Kappock, T J]]
		+	[[Category: Murphy, J R]]
		+	[[Category: Acidophile]]
		+	[[Category: Transferase]]
		+	[[Category: Tricarboxylic acid cycle]]

OCA at 02:13, 1 December 2015

OCA — Tue, 01 Dec 2015 02:13:26 GMT

←Older revision		Revision as of 02:13, 1 December 2015
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5dw5 is ON HOLD	+	The entry 5dw5 is ON HOLD until Paper Publication

	Authors: Kappock, T.J., Murphy, J.R.		Authors: Kappock, T.J., Murphy, J.R.

OCA: Protected "5dw5" [edit=sysop:move=sysop]

OCA — Wed, 30 Sep 2015 13:36:34 GMT

Protected "5dw5" [edit=sysop:move=sysop]

←Older revision

Revision as of 13:36, 30 September 2015

OCA: New page: '''Unreleased structure''' The entry 5dw5 is ON HOLD Authors: Kappock, T.J., Murphy, J.R. Description: Category: Unreleased Structures Category: Murphy, J.R [[Category: Kappoc...

OCA — Wed, 30 Sep 2015 13:36:33 GMT

New page: '''Unreleased structure''' The entry 5dw5 is ON HOLD Authors: Kappock, T.J., Murphy, J.R. Description: Category: Unreleased Structures Category: Murphy, J.R [[Category: Kappoc...

New page

'''Unreleased structure'''

The entry 5dw5 is ON HOLD

Authors: Kappock, T.J., Murphy, J.R.

Description:
[[Category: Unreleased Structures]]
[[Category: Murphy, J.R]]
[[Category: Kappock, T.J]]