4p69 - Revision history

OCA at 00:40, 28 December 2023

OCA — Thu, 28 Dec 2023 00:40:33 GMT

←Older revision		Revision as of 00:40, 28 December 2023
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4p69]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P69 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P69 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4p69]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P69 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P69 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</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]] 3.3Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</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=4p69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p69 OCA], [https://pdbe.org/4p69 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p69 RCSB], [https://www.ebi.ac.uk/pdbsum/4p69 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p69 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=4p69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p69 OCA], [https://pdbe.org/4p69 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p69 RCSB], [https://www.ebi.ac.uk/pdbsum/4p69 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p69 ProSAT]</span></td></tr>
	</table>		</table>

OCA at 12:44, 1 February 2023

OCA — Wed, 01 Feb 2023 12:44:00 GMT

←Older revision		Revision as of 12:44, 1 February 2023
Line 1:		Line 1:

	==Acek (D477A) ICDH complex==		==Acek (D477A) ICDH complex==
-	<StructureSection load='4p69' size='340' side='right' caption='[[4p69]], [[Resolution\|resolution]] 3.30Å' scene=''>	+	<StructureSection load='4p69' size='340' side='right'caption='[[4p69]], [[Resolution\|resolution]] 3.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4p69]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Eco57 Eco57~~] and [~~http~~://en.wikipedia.org/wiki/~~Ecoli Ecoli~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P69 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4P69 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4p69]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P69 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P69 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">aceK, Z5602, ECs4934 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57]), icd, icdA, icdE, b1136, JW1122 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=4p69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p69 OCA], [https://pdbe.org/4p69 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p69 RCSB], [https://www.ebi.ac.uk/pdbsum/4p69 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p69 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/Isocitrate_dehydrogenase_(NADP(+)) Isocitrate dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.42 1.1.1.42] </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=4p69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p69 OCA], [~~http~~://pdbe.org/4p69 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4p69 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4p69 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4p69 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/ACEK_ECO57 ACEK_ECO57]] Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.	+	[https://www.uniprot.org/uniprot/ACEK_ECO57 ACEK_ECO57] Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 22:		Line 20:

	==See Also==		==See Also==
-	*[[Isocitrate dehydrogenase\|Isocitrate dehydrogenase]]	+	*[[Isocitrate dehydrogenase 3D structures\|Isocitrate dehydrogenase 3D structures]]
	*[[Isocitrate dehydrogenase kinase/phosphatase\|Isocitrate dehydrogenase kinase/phosphatase]]		*[[Isocitrate dehydrogenase kinase/phosphatase\|Isocitrate dehydrogenase kinase/phosphatase]]
	== References ==		== References ==
Line 28:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Eco57~~]]	+	[[Category: Escherichia coli K-12]]
-	[[Category: ~~Ecoli~~]]	+	[[Category: Escherichia coli O157:H7]]
-	[[Category: Jimin, Z]]	+	[[Category: Large Structures]]
-	[[Category: Nan, W]]	+	[[Category: Jimin Z]]
-	[[Category: Shu, W]]	+	[[Category: Nan W]]
-	[[Category: Zongchao, J]]	+	[[Category: Shu W]]
-	~~[[Category: Hydrolase-oxidoreductase complex]]~~	+	[[Category: Zongchao J]]
-	~~[[Category: Transferase~~]]	+

OCA at 06:36, 18 October 2018

OCA — Thu, 18 Oct 2018 06:36:43 GMT

←Older revision		Revision as of 06:36, 18 October 2018
Line 22:		Line 22:

	==See Also==		==See Also==
		+	*[[Isocitrate dehydrogenase\|Isocitrate dehydrogenase]]
	*[[Isocitrate dehydrogenase kinase/phosphatase\|Isocitrate dehydrogenase kinase/phosphatase]]		*[[Isocitrate dehydrogenase kinase/phosphatase\|Isocitrate dehydrogenase kinase/phosphatase]]
	== References ==		== References ==

OCA at 05:42, 16 May 2018

OCA — Wed, 16 May 2018 05:42:55 GMT

←Older revision		Revision as of 05:42, 16 May 2018
Line 11:		Line 11:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/ACEK_ECO57 ACEK_ECO57]] Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.		[[http://www.uniprot.org/uniprot/ACEK_ECO57 ACEK_ECO57]] Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	We have revealed that bifunctional AceK kinase/phosphatase utilizes a stepwise addition-elimination mechanism in its dephosphorylation reaction. This work explains how AceK enables opposite kinase and phosphatase activities with Asp477 and a single Mg(2+) ion.
		+
		+	The phosphatase mechanism of bifunctional kinase/phosphatase AceK.,Wang S, Shen Q, Chen G, Zheng J, Tan H, Jia Z Chem Commun (Camb). 2014 Nov 25;50(91):14117-20. doi: 10.1039/c4cc05375c. PMID:25272278<ref>PMID:25272278</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4p69" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Isocitrate dehydrogenase kinase/phosphatase\|Isocitrate dehydrogenase kinase/phosphatase]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 08:34, 22 November 2017

OCA — Wed, 22 Nov 2017 08:34:25 GMT

←Older revision		Revision as of 08:34, 22 November 2017
Line 3:		Line 3:
	<StructureSection load='4p69' size='340' side='right' caption='[[4p69]], [[Resolution\|resolution]] 3.30Å' scene=''>		<StructureSection load='4p69' size='340' side='right' caption='[[4p69]], [[Resolution\|resolution]] 3.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4p69]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P69 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P69 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4p69]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Eco57 Eco57] and [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P69 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P69 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">aceK, Z5602, ECs4934 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57]), icd, icdA, icdE, b1136, JW1122 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Isocitrate_dehydrogenase_(NADP(+)) Isocitrate dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.42 1.1.1.42] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Isocitrate_dehydrogenase_(NADP(+)) Isocitrate dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.42 1.1.1.42] </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=4p69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p69 OCA], [http://pdbe.org/4p69 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4p69 RCSB], [http://www.ebi.ac.uk/pdbsum/4p69 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4p69 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=4p69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p69 OCA], [http://pdbe.org/4p69 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4p69 RCSB], [http://www.ebi.ac.uk/pdbsum/4p69 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4p69 ProSAT]</span></td></tr>
Line 10:		Line 11:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/ACEK_ECO57 ACEK_ECO57]] Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.		[[http://www.uniprot.org/uniprot/ACEK_ECO57 ACEK_ECO57]] Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.
-
-	==See Also==
-	*[[Isocitrate dehydrogenase kinase/phosphatase\|Isocitrate dehydrogenase kinase/phosphatase]]
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Eco57]]
		+	[[Category: Ecoli]]
	[[Category: Jimin, Z]]		[[Category: Jimin, Z]]
	[[Category: Nan, W]]		[[Category: Nan, W]]

OCA at 17:28, 5 August 2016

OCA — Fri, 05 Aug 2016 17:28:18 GMT

←Older revision		Revision as of 17:28, 5 August 2016
Line 1:		Line 1:
		+
	==Acek (D477A) ICDH complex==		==Acek (D477A) ICDH complex==
	<StructureSection load='4p69' size='340' side='right' caption='[[4p69]], [[Resolution\|resolution]] 3.30Å' scene=''>		<StructureSection load='4p69' size='340' side='right' caption='[[4p69]], [[Resolution\|resolution]] 3.30Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Isocitrate_dehydrogenase_(NADP(+)) Isocitrate dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.42 1.1.1.42] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Isocitrate_dehydrogenase_(NADP(+)) Isocitrate dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.42 1.1.1.42] </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=4p69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p69 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4p69 RCSB], [http://www.ebi.ac.uk/pdbsum/4p69 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=4p69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p69 OCA], [http://pdbe.org/4p69 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4p69 RCSB], [http://www.ebi.ac.uk/pdbsum/4p69 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4p69 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/ACEK_ECO57 ACEK_ECO57]] Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.		[[http://www.uniprot.org/uniprot/ACEK_ECO57 ACEK_ECO57]] Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.
		+
		+	==See Also==
		+	*[[Isocitrate dehydrogenase kinase/phosphatase\|Isocitrate dehydrogenase kinase/phosphatase]]
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 20:38, 25 December 2014

OCA — Thu, 25 Dec 2014 20:38:18 GMT

←Older revision		Revision as of 20:38, 25 December 2014
Line 7:		Line 7:
	<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=4p69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p69 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4p69 RCSB], [http://www.ebi.ac.uk/pdbsum/4p69 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=4p69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p69 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4p69 RCSB], [http://www.ebi.ac.uk/pdbsum/4p69 PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ACEK_ECO57 ACEK_ECO57]] Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Jimin, Z.]]	+	[[Category: Jimin, Z]]
-	[[Category: Nan, W.]]	+	[[Category: Nan, W]]
-	[[Category: Shu, W.]]	+	[[Category: Shu, W]]
-	[[Category: Zongchao, J.]]	+	[[Category: Zongchao, J]]
	[[Category: Hydrolase-oxidoreductase complex]]		[[Category: Hydrolase-oxidoreductase complex]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 07:51, 8 October 2014

OCA — Wed, 08 Oct 2014 07:51:37 GMT

←Older revision		Revision as of 07:51, 8 October 2014
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==Acek (D477A) ICDH complex==
-		+	<StructureSection load='4p69' size='340' side='right' caption='[[4p69]], [[Resolution\|resolution]] 3.30Å' scene=''>
-	~~The entry~~ 4p69 is ~~ON HOLD~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4p69]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P69 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P69 FirstGlance]. <br>
-	~~Authors~~: Jimin, Z., Nan, W., Shu, W., Zongchao, J.	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene></td></tr>
-		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Isocitrate_dehydrogenase_(NADP(+)) Isocitrate dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.42 1.1.1.42] </span></td></tr>
-	~~Description~~: ~~Acek (D477A) ICDH~~ complex	+	<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=4p69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p69 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4p69 RCSB], [http://www.ebi.ac.uk/pdbsum/4p69 PDBsum]</span></td></tr>
		+	</table>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Jimin, Z.]]
		+	[[Category: Nan, W.]]
		+	[[Category: Shu, W.]]
		+	[[Category: Zongchao, J.]]
		+	[[Category: Hydrolase-oxidoreductase complex]]
		+	[[Category: Transferase]]

OCA at 03:52, 4 September 2014

OCA — Thu, 04 Sep 2014 03:52:26 GMT

←Older revision		Revision as of 03:52, 4 September 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4p69 is ON HOLD ~~until sometime in the future~~	+	The entry 4p69 is ON HOLD

	Authors: Jimin, Z., Nan, W., Shu, W., Zongchao, J.		Authors: Jimin, Z., Nan, W., Shu, W., Zongchao, J.

-	Description: Acek(D477A) ICDH complex	+	Description: Acek (D477A) ICDH complex

OCA at 14:21, 20 August 2014

OCA — Wed, 20 Aug 2014 14:21:30 GMT

←Older revision		Revision as of 14:21, 20 August 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4p69 is ON HOLD	+	The entry 4p69 is ON HOLD until sometime in the future

	Authors: Jimin, Z., Nan, W., Shu, W., Zongchao, J.		Authors: Jimin, Z., Nan, W., Shu, W., Zongchao, J.

	Description: Acek(D477A) ICDH complex		Description: Acek(D477A) ICDH complex