4c3k - Revision history

OCA at 12:02, 20 December 2023

2023-12-20T12:02:51Z

←Older revision		Revision as of 12:02, 20 December 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4c3k]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_elongatus Synechococcus elongatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C3K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C3K FirstGlance]. <br>		<table><tr><td colspan='2'>[[4c3k]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_elongatus Synechococcus elongatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C3K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C3K 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=PO4:PHOSPHATE+ION'>PO4</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]] 3.099Å</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=PO4:PHOSPHATE+ION'>PO4</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=4c3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c3k OCA], [https://pdbe.org/4c3k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c3k RCSB], [https://www.ebi.ac.uk/pdbsum/4c3k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c3k 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=4c3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c3k OCA], [https://pdbe.org/4c3k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c3k RCSB], [https://www.ebi.ac.uk/pdbsum/4c3k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c3k ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/GLNB_SYNE7 GLNB_SYNE7]] P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is phosphorylated, these events are reversed. In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is phosphorylated which allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme.	+	[https://www.uniprot.org/uniprot/GLNB_SYNE7 GLNB_SYNE7] P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is phosphorylated, these events are reversed. In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is phosphorylated which allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	PII signaling proteins comprise one of the most versatile signaling devices in nature and have a highly conserved structure. In cyanobacteria, PipX and N-acetyl-L-glutamate kinase (NAGK) are receptors of PII signaling, and these interactions are modulated by ADP, ATP, and 2-oxoglutarate. These effector molecules bind interdependently to three anti-cooperative binding sites on the trimeric PII protein and thereby affect its structure. Here, we used the PII protein from Synechococcus elongatus PCC 7942 to reveal the structural basis of anti-cooperative ADP binding. Furthermore, we clarified the mutual influence of PII-receptor interaction and sensing of the ATP/ADP ratio. The crystal structures of two forms of trimeric PII - one with one ADP bound and the other with all three ADP-binding sites occupied - revealed significant differences in the ADP binding mode: at one site (S1), ADP is tightly bound through side-chain and main-chain interactions, whereas at the other two sites (S2 and S3), the ADP molecules are only bound by main-chain interactions. In the presence of the PII-receptor PipX, the affinity of ADP to the first binding site S1 strongly increases, whereas the affinity for ATP decreases owing to PipX favoring the S1 conformation of PII-ADP. In consequence, PII-PipX interaction is highly sensitive to subtle fluctuations in the ATP/ADP ratio. By contrast, the PII-NAGK interaction, which is negatively affected by ADP, is insensitive to these fluctuations. Modulation of the metabolite-sensing properties of PII by its receptors allows PII to differentially perceive signals in a target-specific manner and to perform multitasking signal transduction.
		+
		+	Structural Basis and Target-Specific Modulation of ADP Sensing by the Synechococcus elongatus PII Signaling Protein.,Zeth K, Fokina O, Forchhammer K J Biol Chem. 2014 Feb 11. PMID:24519945<ref>PMID:24519945</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4c3k" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Beta-lactamase 3D structures\|Beta-lactamase 3D structures]]		*[[Beta-lactamase 3D structures\|Beta-lactamase 3D structures]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 17:24, 7 September 2022

2022-09-07T17:24:24Z

←Older revision		Revision as of 17:24, 7 September 2022
Line 3:		Line 3:
	<StructureSection load='4c3k' size='340' side='right'caption='[[4c3k]], [[Resolution\|resolution]] 3.10Å' scene=''>		<StructureSection load='4c3k' size='340' side='right'caption='[[4c3k]], [[Resolution\|resolution]] 3.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4c3k]] is a 6 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Pcc_6301 Pcc 6301~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C3K OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4C3K FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4c3k]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_elongatus Synechococcus elongatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C3K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C3K 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=PO4:PHOSPHATE+ION'>PO4</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=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c3l\|4c3l]], [[4c3m\|4c3m]]~~</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=4c3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c3k OCA], [https://pdbe.org/4c3k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c3k RCSB], [https://www.ebi.ac.uk/pdbsum/4c3k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c3k 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=4c3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c3k OCA], [~~http~~://pdbe.org/4c3k PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4c3k RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4c3k PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4c3k ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/GLNB_SYNE7 GLNB_SYNE7]] P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is phosphorylated, these events are reversed. In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is phosphorylated which allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme.	+	[[https://www.uniprot.org/uniprot/GLNB_SYNE7 GLNB_SYNE7]] P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is phosphorylated, these events are reversed. In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is phosphorylated which allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme.
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	PII signaling proteins comprise one of the most versatile signaling devices in nature and have a highly conserved structure. In cyanobacteria, PipX and N-acetyl-L-glutamate kinase (NAGK) are receptors of PII signaling, and these interactions are modulated by ADP, ATP, and 2-oxoglutarate. These effector molecules bind interdependently to three anti-cooperative binding sites on the trimeric PII protein and thereby affect its structure. Here, we used the PII protein from Synechococcus elongatus PCC 7942 to reveal the structural basis of anti-cooperative ADP binding. Furthermore, we clarified the mutual influence of PII-receptor interaction and sensing of the ATP/ADP ratio. The crystal structures of two forms of trimeric PII - one with one ADP bound and the other with all three ADP-binding sites occupied - revealed significant differences in the ADP binding mode: at one site (S1), ADP is tightly bound through side-chain and main-chain interactions, whereas at the other two sites (S2 and S3), the ADP molecules are only bound by main-chain interactions. In the presence of the PII-receptor PipX, the affinity of ADP to the first binding site S1 strongly increases, whereas the affinity for ATP decreases owing to PipX favoring the S1 conformation of PII-ADP. In consequence, PII-PipX interaction is highly sensitive to subtle fluctuations in the ATP/ADP ratio. By contrast, the PII-NAGK interaction, which is negatively affected by ADP, is insensitive to these fluctuations. Modulation of the metabolite-sensing properties of PII by its receptors allows PII to differentially perceive signals in a target-specific manner and to perform multitasking signal transduction.	+
-		+
-	Structural Basis and Target-Specific Modulation of ADP Sensing by the Synechococcus elongatus PII Signaling Protein.,Zeth K, Fokina O, Forchhammer K J Biol Chem. 2014 Feb 11. PMID:24519945<ref>PMID:24519945</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 4c3k" style="background-color:#fffaf0;"></div>~~	+

	==See Also==		==See Also==
-	*[[Beta-lactamase\|Beta-lactamase]]	+	*[[Beta-lactamase 3D structures\|Beta-lactamase 3D structures]]
-	~~== References ==~~	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Pcc 6301~~]]	+	[[Category: Synechococcus elongatus]]
-	[[Category: Forchhammer, K]]	+	[[Category: Forchhammer K]]
-	[[Category: Zeth, K]]	+	[[Category: Zeth K]]
-	~~[[Category: Transcription~~]]	+

OCA at 09:00, 20 March 2019

2019-03-20T09:00:09Z

←Older revision		Revision as of 09:00, 20 March 2019
Line 1:		Line 1:

	==Structure of mixed PII-ADP complexes from S. elongatus==		==Structure of mixed PII-ADP complexes from S. elongatus==
-	<StructureSection load='4c3k' size='340' side='right' caption='[[4c3k]], [[Resolution\|resolution]] 3.10Å' scene=''>	+	<StructureSection load='4c3k' size='340' side='right'caption='[[4c3k]], [[Resolution\|resolution]] 3.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4c3k]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Pcc_6301 Pcc 6301]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C3K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C3K FirstGlance]. <br>		<table><tr><td colspan='2'>[[4c3k]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Pcc_6301 Pcc 6301]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C3K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C3K FirstGlance]. <br>
Line 26:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Pcc 6301]]		[[Category: Pcc 6301]]
	[[Category: Forchhammer, K]]		[[Category: Forchhammer, K]]
	[[Category: Zeth, K]]		[[Category: Zeth, K]]
	[[Category: Transcription]]		[[Category: Transcription]]

OCA at 18:10, 4 August 2016

2016-08-04T18:10:02Z

←Older revision		Revision as of 18:10, 4 August 2016
Line 1:		Line 1:
		+
	==Structure of mixed PII-ADP complexes from S. elongatus==		==Structure of mixed PII-ADP complexes from S. elongatus==
	<StructureSection load='4c3k' size='340' side='right' caption='[[4c3k]], [[Resolution\|resolution]] 3.10Å' scene=''>		<StructureSection load='4c3k' size='340' side='right' caption='[[4c3k]], [[Resolution\|resolution]] 3.10Å' 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=PO4:PHOSPHATE+ION'>PO4</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=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c3l\|4c3l]], [[4c3m\|4c3m]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c3l\|4c3l]], [[4c3m\|4c3m]]</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=4c3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c3k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c3k RCSB], [http://www.ebi.ac.uk/pdbsum/4c3k 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=4c3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c3k OCA], [http://pdbe.org/4c3k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c3k RCSB], [http://www.ebi.ac.uk/pdbsum/4c3k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c3k ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	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 4c3k" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Beta-lactamase\|Beta-lactamase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 11:46, 25 December 2014

2014-12-25T11:46:28Z

←Older revision		Revision as of 11:46, 25 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4c3k\| PDB=4c3k \| SCENE= }}~~	+	==Structure of mixed PII-ADP complexes from S. elongatus==
-	===Structure of mixed PII-ADP complexes from S. elongatus===	+	<StructureSection load='4c3k' size='340' side='right' caption='[[4c3k]], [[Resolution\|resolution]] 3.10Å' scene=''>
-	~~{{ABSTRACT_PUBMED_24519945}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4c3k]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Pcc_6301 Pcc 6301]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C3K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C3K FirstGlance]. <br>
-	==Function==	+	</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=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c3l\|4c3l]], [[4c3m\|4c3m]]</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=4c3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c3k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c3k RCSB], [http://www.ebi.ac.uk/pdbsum/4c3k PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
	[[http://www.uniprot.org/uniprot/GLNB_SYNE7 GLNB_SYNE7]] P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is phosphorylated, these events are reversed. In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is phosphorylated which allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme.		[[http://www.uniprot.org/uniprot/GLNB_SYNE7 GLNB_SYNE7]] P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is phosphorylated, these events are reversed. In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is phosphorylated which allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	PII signaling proteins comprise one of the most versatile signaling devices in nature and have a highly conserved structure. In cyanobacteria, PipX and N-acetyl-L-glutamate kinase (NAGK) are receptors of PII signaling, and these interactions are modulated by ADP, ATP, and 2-oxoglutarate. These effector molecules bind interdependently to three anti-cooperative binding sites on the trimeric PII protein and thereby affect its structure. Here, we used the PII protein from Synechococcus elongatus PCC 7942 to reveal the structural basis of anti-cooperative ADP binding. Furthermore, we clarified the mutual influence of PII-receptor interaction and sensing of the ATP/ADP ratio. The crystal structures of two forms of trimeric PII - one with one ADP bound and the other with all three ADP-binding sites occupied - revealed significant differences in the ADP binding mode: at one site (S1), ADP is tightly bound through side-chain and main-chain interactions, whereas at the other two sites (S2 and S3), the ADP molecules are only bound by main-chain interactions. In the presence of the PII-receptor PipX, the affinity of ADP to the first binding site S1 strongly increases, whereas the affinity for ATP decreases owing to PipX favoring the S1 conformation of PII-ADP. In consequence, PII-PipX interaction is highly sensitive to subtle fluctuations in the ATP/ADP ratio. By contrast, the PII-NAGK interaction, which is negatively affected by ADP, is insensitive to these fluctuations. Modulation of the metabolite-sensing properties of PII by its receptors allows PII to differentially perceive signals in a target-specific manner and to perform multitasking signal transduction.

-	~~==About this Structure==~~	+	Structural Basis and Target-Specific Modulation of ADP Sensing by the Synechococcus elongatus PII Signaling Protein.,Zeth K, Fokina O, Forchhammer K J Biol Chem. 2014 Feb 11. PMID:24519945<ref>PMID:24519945</ref>
-	~~[[4c3k]] is a 6 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Pcc_6301 Pcc 6301]~~. ~~Full crystallographic information is available from [http~~:/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=4C3K OCA].~~	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:024519945</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Pcc 6301]]		[[Category: Pcc 6301]]
-	[[Category: Forchhammer, K.]]	+	[[Category: Forchhammer, K]]
-	[[Category: Zeth, K.]]	+	[[Category: Zeth, K]]
	[[Category: Transcription]]		[[Category: Transcription]]

OCA at 07:55, 16 April 2014

2014-04-16T07:55:24Z

←Older revision		Revision as of 07:55, 16 April 2014
Line 7:		Line 7:

	==About this Structure==		==About this Structure==
-	[[4c3k]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C3K OCA].	+	[[4c3k]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Pcc_6301 Pcc 6301]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C3K OCA].

	==Reference==		==Reference==
	<ref group="xtra">PMID:024519945</ref><references group="xtra"/><references/>		<ref group="xtra">PMID:024519945</ref><references group="xtra"/><references/>
		+	[[Category: Pcc 6301]]
	[[Category: Forchhammer, K.]]		[[Category: Forchhammer, K.]]
	[[Category: Zeth, K.]]		[[Category: Zeth, K.]]
	[[Category: Transcription]]		[[Category: Transcription]]

OCA at 14:43, 19 February 2014

2014-02-19T14:43:24Z

←Older revision		Revision as of 14:43, 19 February 2014
Line 1:		Line 1:
	{{STRUCTURE_4c3k\| PDB=4c3k \| SCENE= }}		{{STRUCTURE_4c3k\| PDB=4c3k \| SCENE= }}
	===Structure of mixed PII-ADP complexes from S. elongatus===		===Structure of mixed PII-ADP complexes from S. elongatus===
		+	{{ABSTRACT_PUBMED_24519945}}

	==Function==		==Function==
Line 7:		Line 8:
	==About this Structure==		==About this Structure==
	[[4c3k]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C3K OCA].		[[4c3k]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C3K OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:024519945</ref><references group="xtra"/><references/>
	[[Category: Forchhammer, K.]]		[[Category: Forchhammer, K.]]
	[[Category: Zeth, K.]]		[[Category: Zeth, K.]]
	[[Category: Transcription]]		[[Category: Transcription]]

OCA at 05:14, 13 February 2014

2014-02-13T05:14:26Z

←Older revision		Revision as of 05:14, 13 February 2014
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_4c3k\| PDB=4c3k \| SCENE= }}
		+	===Structure of mixed PII-ADP complexes from S. elongatus===

-	~~The entry 4c3k~~ is ~~ON HOLD until sometime in~~ the ~~future~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/GLNB_SYNE7 GLNB_SYNE7]] P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is phosphorylated, these events are reversed. In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is phosphorylated which allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme.

-	~~Authors~~: ~~Zeth, K~~., Forchhammer, K.	+	==About this Structure==
-		+	[[4c3k]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C3K OCA].
-	~~Description~~: ~~Structure of mixed PII-ADP complexes from S~~. ~~elongatus~~	+	[[Category: Forchhammer, K.]]
		+	[[Category: Zeth, K.]]
		+	[[Category: Transcription]]

OCA at 09:43, 5 February 2014

2014-02-05T09:43:17Z

←Older revision		Revision as of 09:43, 5 February 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4c3k is ON HOLD	+	The entry 4c3k is ON HOLD until sometime in the future

	Authors: Zeth, K., Forchhammer, K.		Authors: Zeth, K., Forchhammer, K.

	Description: Structure of mixed PII-ADP complexes from S. elongatus		Description: Structure of mixed PII-ADP complexes from S. elongatus

OCA: Protected "4c3k" [edit=sysop:move=sysop]

2013-09-04T09:31:34Z

Protected "4c3k" [edit=sysop:move=sysop]

←Older revision

Revision as of 09:31, 4 September 2013