4o99 - Revision history

OCA at 14:54, 8 November 2023

2023-11-08T14:54:56Z

←Older revision		Revision as of 14:54, 8 November 2023
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4o99]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Cupriavidus_necator_H16 Cupriavidus necator H16]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O99 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O99 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4o99]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Cupriavidus_necator_H16 Cupriavidus necator H16]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O99 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O99 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.96Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=4o99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o99 OCA], [https://pdbe.org/4o99 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o99 RCSB], [https://www.ebi.ac.uk/pdbsum/4o99 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o99 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=4o99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o99 OCA], [https://pdbe.org/4o99 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o99 RCSB], [https://www.ebi.ac.uk/pdbsum/4o99 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o99 ProSAT]</span></td></tr>
	</table>		</table>

OCA at 07:12, 25 January 2023

2023-01-25T07:12:42Z

←Older revision		Revision as of 07:12, 25 January 2023
Line 1:		Line 1:

	==Crystal structure of Beta-ketothiolase (PhaA) from Ralstonia eutropha H16==		==Crystal structure of Beta-ketothiolase (PhaA) from Ralstonia eutropha H16==
-	<StructureSection load='4o99' size='340' side='right' caption='[[4o99]], [[Resolution\|resolution]] 1.96Å' scene=''>	+	<StructureSection load='4o99' size='340' side='right'caption='[[4o99]], [[Resolution\|resolution]] 1.96Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4o99]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Alcaligenes_eutropha_h16 Alcaligenes eutropha h16~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O99 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4O99 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4o99]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Cupriavidus_necator_H16 Cupriavidus necator H16]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O99 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O99 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4o9a\|4o9a]], [[4o9c\|4o9c]]</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=4o99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o99 OCA], [https://pdbe.org/4o99 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o99 RCSB], [https://www.ebi.ac.uk/pdbsum/4o99 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o99 ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">H16_A1438, phaA, phbA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=381666 Alcaligenes eutropha H16])</td></tr>	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetyl-CoA_C-acetyltransferase Acetyl-CoA C-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.9 2.3.1.9] </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=4o99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o99 OCA], [~~http~~://pdbe.org/4o99 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4o99 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4o99 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4o99 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/THIL_CUPNH THIL_CUPNH]] Catalyzes the condensation of two acetyl-coA units to form acetoacetyl-CoA. Is involved in the biosynthesis of polyhydroxybutyrate (PHB), which is accumulated as an intracellular energy reserve material when cells grow under conditions of nutrient limitation. Also catalyzes the reverse reaction, i.e. the cleavage of acetoacetyl-CoA, and is therefore also involved in the reutilization of PHB.<ref>PMID:2670935</ref> <ref>PMID:2670936</ref> <ref>PMID:4198758</ref>	+	[https://www.uniprot.org/uniprot/THIL_CUPNH THIL_CUPNH] Catalyzes the condensation of two acetyl-coA units to form acetoacetyl-CoA. Is involved in the biosynthesis of polyhydroxybutyrate (PHB), which is accumulated as an intracellular energy reserve material when cells grow under conditions of nutrient limitation. Also catalyzes the reverse reaction, i.e. the cleavage of acetoacetyl-CoA, and is therefore also involved in the reutilization of PHB.<ref>PMID:2670935</ref> <ref>PMID:2670936</ref> <ref>PMID:4198758</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 4o99" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4o99" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Thiolase 3D structures\|Thiolase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Acetyl-CoA C-acetyltransferase~~]]	+	[[Category: Cupriavidus necator H16]]
-	[[Category: ~~Alcaligenes eutropha h16~~]]	+	[[Category: Large Structures]]
-	[[Category: Kim~~, E J~~]]	+	[[Category: Kim EJ]]
-	[[Category: Kim, J]]	+	[[Category: Kim J]]
-	[[Category: Kim~~, K J~~]]	+	[[Category: Kim KJ]]
-	[[Category: Kim, S]]	+	[[Category: Kim S]]
-	~~[[Category: Acetoacetyl-coa transferase]]~~	+
-	~~[[Category: Acyltransferase transferase]]~~	+
-	~~[[Category: Phb biosynthesis]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 08:22, 22 November 2017

2017-11-22T08:22:33Z

←Older revision		Revision as of 08:22, 22 November 2017
Line 3:		Line 3:
	<StructureSection load='4o99' size='340' side='right' caption='[[4o99]], [[Resolution\|resolution]] 1.96Å' scene=''>		<StructureSection load='4o99' size='340' side='right' caption='[[4o99]], [[Resolution\|resolution]] 1.96Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4o99]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O99 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O99 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4o99]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Alcaligenes_eutropha_h16 Alcaligenes eutropha h16]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O99 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O99 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4o9a\|4o9a]], [[4o9c\|4o9c]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4o9a\|4o9a]], [[4o9c\|4o9c]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">H16_A1438, phaA, phbA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=381666 Alcaligenes eutropha H16])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetyl-CoA_C-acetyltransferase Acetyl-CoA C-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.9 2.3.1.9] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetyl-CoA_C-acetyltransferase Acetyl-CoA C-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.9 2.3.1.9] </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=4o99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o99 OCA], [http://pdbe.org/4o99 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4o99 RCSB], [http://www.ebi.ac.uk/pdbsum/4o99 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4o99 ProSAT]</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=4o99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o99 OCA], [http://pdbe.org/4o99 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4o99 RCSB], [http://www.ebi.ac.uk/pdbsum/4o99 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4o99 ProSAT]</span></td></tr>
Line 25:		Line 26:
	</StructureSection>		</StructureSection>
	[[Category: Acetyl-CoA C-acetyltransferase]]		[[Category: Acetyl-CoA C-acetyltransferase]]
		+	[[Category: Alcaligenes eutropha h16]]
	[[Category: Kim, E J]]		[[Category: Kim, E J]]
	[[Category: Kim, J]]		[[Category: Kim, J]]

OCA at 14:10, 4 August 2016

2016-08-04T14:10:16Z

←Older revision		Revision as of 14:10, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of Beta-ketothiolase (PhaA) from Ralstonia eutropha H16==		==Crystal structure of Beta-ketothiolase (PhaA) from Ralstonia eutropha H16==
	<StructureSection load='4o99' size='340' side='right' caption='[[4o99]], [[Resolution\|resolution]] 1.96Å' scene=''>		<StructureSection load='4o99' size='340' side='right' caption='[[4o99]], [[Resolution\|resolution]] 1.96Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4o9a\|4o9a]], [[4o9c\|4o9c]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4o9a\|4o9a]], [[4o9c\|4o9c]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetyl-CoA_C-acetyltransferase Acetyl-CoA C-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.9 2.3.1.9] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetyl-CoA_C-acetyltransferase Acetyl-CoA C-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.9 2.3.1.9] </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=4o99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o99 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o99 RCSB], [http://www.ebi.ac.uk/pdbsum/4o99 PDBsum]</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=4o99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o99 OCA], [http://pdbe.org/4o99 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4o99 RCSB], [http://www.ebi.ac.uk/pdbsum/4o99 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4o99 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	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>
	</div>		</div>
		+	<div class="pdbe-citations 4o99" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 15:28, 24 December 2014

2014-12-24T15:28:17Z

←Older revision		Revision as of 15:28, 24 December 2014
Line 8:		Line 8:
	<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=4o99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o99 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o99 RCSB], [http://www.ebi.ac.uk/pdbsum/4o99 PDBsum]</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=4o99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o99 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o99 RCSB], [http://www.ebi.ac.uk/pdbsum/4o99 PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/THIL_CUPNH THIL_CUPNH]] Catalyzes the condensation of two acetyl-coA units to form acetoacetyl-CoA. Is involved in the biosynthesis of polyhydroxybutyrate (PHB), which is accumulated as an intracellular energy reserve material when cells grow under conditions of nutrient limitation. Also catalyzes the reverse reaction, i.e. the cleavage of acetoacetyl-CoA, and is therefore also involved in the reutilization of PHB.<ref>PMID:2670935</ref> <ref>PMID:2670936</ref> <ref>PMID:4198758</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 12:48, 17 December 2014

2014-12-17T12:48:12Z

←Older revision		Revision as of 12:48, 17 December 2014
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==Crystal structure of Beta-ketothiolase (PhaA) from Ralstonia eutropha H16==
		+	<StructureSection load='4o99' size='340' side='right' caption='[[4o99]], [[Resolution\|resolution]] 1.96Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4o99]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O99 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O99 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4o9a\|4o9a]], [[4o9c\|4o9c]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetyl-CoA_C-acetyltransferase Acetyl-CoA C-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.9 2.3.1.9] </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=4o99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o99 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o99 RCSB], [http://www.ebi.ac.uk/pdbsum/4o99 PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	PhaA from Ralstonia eutropha (RePhaA) is the first enzyme in the polyhydroxyalbutyrate (PHB) biosynthetic pathway and catalyzes the condensation of two molecules of acetyl-CoA to acetoacetyl-CoA. To investigate the molecular mechanism underlying PHB biosynthesis, we determined the crystal structures of the RePhaA protein in apo- and CoA-bound forms. The RePhaA structure adopts the type II biosynthetic thiolase fold forming a tetramer by means of dimerization of two dimers. The crystal structure of RePhaA in complex with CoA revealed that the enzyme contained a unique Phe219 residue, resulting that the ADP moiety binds in somewhat different position compared with that bound in other thiolase enzymes. Our study provides structural insight into the substrate specificity of RePhaA. Results indicate the presence of a small pocket near the Cys88 covalent catalytic residue leading to the possibility of the enzyme to accommodate acetyl-CoA as a sole substrate instead of larger acyl-CoA molecules such as propionyl-CoA. Furthermore, the roles of key residues involved in substrate binding and enzyme catalysis were confirmed by site-directed mutagenesis.

-	~~The entry 4o99 is ON HOLD until Paper Publication~~	+	Crystal structure and biochemical characterization of PhaA from Ralstonia eutropha, a polyhydroxyalkanoate-producing bacterium.,Kim EJ, Kim KJ Biochem Biophys Res Commun. 2014 Sep 12;452(1):124-9. doi:, 10.1016/j.bbrc.2014.08.074. Epub 2014 Aug 21. PMID:25152395<ref>PMID:25152395</ref>

-	~~Authors~~: Kim, E.-J., Kim, J~~., Kim, S.,~~ Kim, K.-J.	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description~~: ~~Crystal structure of Beta~~-~~ketothiolase (PhaA) from Ralstonia eutropha H16~~	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Acetyl-CoA C-acetyltransferase]]
		+	[[Category: Kim, E J]]
		+	[[Category: Kim, J]]
		+	[[Category: Kim, K J]]
		+	[[Category: Kim, S]]
		+	[[Category: Acetoacetyl-coa transferase]]
		+	[[Category: Acyltransferase transferase]]
		+	[[Category: Phb biosynthesis]]
		+	[[Category: Transferase]]

OCA at 06:11, 8 October 2014

2014-10-08T06:11:57Z

←Older revision		Revision as of 06:11, 8 October 2014
Line 3:		Line 3:
	The entry 4o99 is ON HOLD until Paper Publication		The entry 4o99 is ON HOLD until Paper Publication

-	Authors: Kim, E.-J, Kim, J., Kim, S., Kim, K.-J.	+	Authors: Kim, E.-J., Kim, J., Kim, S., Kim, K.-J.

	Description: Crystal structure of Beta-ketothiolase (PhaA) from Ralstonia eutropha H16		Description: Crystal structure of Beta-ketothiolase (PhaA) from Ralstonia eutropha H16

OCA at 16:12, 19 February 2014

2014-02-19T16:12:14Z

←Older revision		Revision as of 16:12, 19 February 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4o99 is ON HOLD	+	The entry 4o99 is ON HOLD until Paper Publication

	Authors: Kim, E.-J, Kim, J., Kim, S., Kim, K.-J.		Authors: Kim, E.-J, Kim, J., Kim, S., Kim, K.-J.

	Description: Crystal structure of Beta-ketothiolase (PhaA) from Ralstonia eutropha H16		Description: Crystal structure of Beta-ketothiolase (PhaA) from Ralstonia eutropha H16

OCA: Protected "4o99" [edit=sysop:move=sysop]

2014-01-08T09:29:19Z

Protected "4o99" [edit=sysop:move=sysop]

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Revision as of 09:29, 8 January 2014

OCA: New page: '''Unreleased structure''' The entry 4o99 is ON HOLD Authors: Kim, E.-J, Kim, J., Kim, S., Kim, K.-J. Description: Crystal structure of Beta-ketothiolase (PhaA) from Ralstonia eutropha...

2014-01-08T09:29:18Z

New page: '''Unreleased structure''' The entry 4o99 is ON HOLD Authors: Kim, E.-J, Kim, J., Kim, S., Kim, K.-J. Description: Crystal structure of Beta-ketothiolase (PhaA) from Ralstonia eutropha...

New page

'''Unreleased structure'''

The entry 4o99 is ON HOLD

Authors: Kim, E.-J, Kim, J., Kim, S., Kim, K.-J.

Description: Crystal structure of Beta-ketothiolase (PhaA) from Ralstonia eutropha H16