4g86 - Revision history

OCA at 11:26, 1 March 2024

2024-03-01T11:26:07Z

← Older revision		Revision as of 11:26, 1 March 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4g86]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_elongatus_PCC_7942_=_FACHB-805 Synechococcus elongatus PCC 7942 = FACHB-805]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G86 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G86 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4g86]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_elongatus_PCC_7942_=_FACHB-805 Synechococcus elongatus PCC 7942 = FACHB-805]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G86 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G86 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=2PE:NONAETHYLENE+GLYCOL'>2PE</scene>, <scene name='pdbligand=BNT:2,5-DIBROMO-3-ISOPROPYL-6-METHYLBENZO-1,4-QUINONE'>BNT</scene>, <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]] 2.387Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=2PE:NONAETHYLENE+GLYCOL'>2PE</scene>, <scene name='pdbligand=BNT:2,5-DIBROMO-3-ISOPROPYL-6-METHYLBENZO-1,4-QUINONE'>BNT</scene>, <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=4g86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g86 OCA], [https://pdbe.org/4g86 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g86 RCSB], [https://www.ebi.ac.uk/pdbsum/4g86 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g86 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=4g86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g86 OCA], [https://pdbe.org/4g86 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g86 RCSB], [https://www.ebi.ac.uk/pdbsum/4g86 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g86 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/KAIA_SYNE7 KAIA_SYNE7] Component of the KaiABC clock protein complex, which constitutes the main circadian regulator in cyanobacteria. The KaiABC complex may act as a promoter-nonspecific transcription regulator that represses transcription, possibly by acting on the state of chromosome compaction. In the complex, it enhances the phosphorylation status of KaiC. In contrast, the presence of KaiB in the complex decreases the phosphorylation status of KaiC, suggesting that KaiB acts by antagonizing the interaction between KaiA and KaiC. A KaiA dimer is sufficient to enhance KaiC hexamer phosphorylation.<ref>PMID:12391300</ref> <ref>PMID:12727878</ref> <ref>PMID:12727879</ref> <ref>PMID:9727980</ref>		[https://www.uniprot.org/uniprot/KAIA_SYNE7 KAIA_SYNE7] Component of the KaiABC clock protein complex, which constitutes the main circadian regulator in cyanobacteria. The KaiABC complex may act as a promoter-nonspecific transcription regulator that represses transcription, possibly by acting on the state of chromosome compaction. In the complex, it enhances the phosphorylation status of KaiC. In contrast, the presence of KaiB in the complex decreases the phosphorylation status of KaiC, suggesting that KaiB acts by antagonizing the interaction between KaiA and KaiC. A KaiA dimer is sufficient to enhance KaiC hexamer phosphorylation.<ref>PMID:12391300</ref> <ref>PMID:12727878</ref> <ref>PMID:12727879</ref> <ref>PMID:9727980</ref>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	KaiA protein that stimulates KaiC phosphorylation in the cyanobacterial circadian clock was recently shown to be destabilized by dibromothymoquinone (DBMIB), thus revealing KaiA as a sensor of the plastoquinone (PQ) redox state and suggesting an indirect control of the clock by light through PQ redox changes. Here we show using X-ray crystallography that several DBMIBs are bound to KaiA dimer. Some binding modes are consistent with oligomerization of N-terminal KaiA pseudoreceiver domains and/or reduced interdomain flexibility. DBMIB bound to the C-terminal KaiA (C-KaiA) domain and limited stimulation of KaiC kinase activity by C-KaiA in the presence of DBMIB demonstrate that the cofactor may weakly inhibit KaiA-KaiC binding.

	Crystal Structure of the Redox-Active Cofactor Dibromothymoquinone Bound to Circadian Clock Protein KaiA and Structural Basis for Dibromothymoquinone's Ability to Prevent Stimulation of KaiC Phosphorylation by KaiA.,Pattanayek R, Sidiqi SK, Egli M Biochemistry. 2012 Oct 5. PMID:23020633<ref>PMID:23020633</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 4g86" style="background-color:#fffaf0;"></div>~~

	==See Also==		==See Also==

OCA at 20:29, 19 October 2022

2022-10-19T20:29:39Z

← Older revision		Revision as of 20:29, 19 October 2022
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	<StructureSection load='4g86' size='340' side='right'caption='[[4g86]], [[Resolution\|resolution]] 2.39Å' scene=''>		<StructureSection load='4g86' size='340' side='right'caption='[[4g86]], [[Resolution\|resolution]] 2.39Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4g86]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Anacystis_nidulans_r2 Anacystis nidulans r2~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G86 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4G86 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4g86]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_elongatus_PCC_7942_=_FACHB-805 Synechococcus elongatus PCC 7942 = FACHB-805]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G86 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G86 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=2PE:NONAETHYLENE+GLYCOL'>2PE</scene>, <scene name='pdbligand=BNT:2,5-DIBROMO-3-ISOPROPYL-6-METHYLBENZO-1,4-QUINONE'>BNT</scene>, <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=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=2PE:NONAETHYLENE+GLYCOL'>2PE</scene>, <scene name='pdbligand=BNT:2,5-DIBROMO-3-ISOPROPYL-6-METHYLBENZO-1,4-QUINONE'>BNT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1r8j\|1r8j]]</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=4g86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g86 OCA], [https://pdbe.org/4g86 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g86 RCSB], [https://www.ebi.ac.uk/pdbsum/4g86 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g86 ProSAT]</span></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">kaiA, see0009, Synpcc7942_1218 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1140 Anacystis nidulans R2])</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=4g86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g86 OCA], [~~http~~://pdbe.org/4g86 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4g86 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4g86 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4g86 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[~~[http~~://www.uniprot.org/uniprot/KAIA_SYNE7 KAIA_SYNE7]] Component of the KaiABC clock protein complex, which constitutes the main circadian regulator in cyanobacteria. The KaiABC complex may act as a promoter-nonspecific transcription regulator that represses transcription, possibly by acting on the state of chromosome compaction. In the complex, it enhances the phosphorylation status of KaiC. In contrast, the presence of KaiB in the complex decreases the phosphorylation status of KaiC, suggesting that KaiB acts by antagonizing the interaction between KaiA and KaiC. A KaiA dimer is sufficient to enhance KaiC hexamer phosphorylation.<ref>PMID:12391300</ref> <ref>PMID:12727878</ref> <ref>PMID:12727879</ref> <ref>PMID:9727980</ref>		[https://www.uniprot.org/uniprot/KAIA_SYNE7 KAIA_SYNE7] Component of the KaiABC clock protein complex, which constitutes the main circadian regulator in cyanobacteria. The KaiABC complex may act as a promoter-nonspecific transcription regulator that represses transcription, possibly by acting on the state of chromosome compaction. In the complex, it enhances the phosphorylation status of KaiC. In contrast, the presence of KaiB in the complex decreases the phosphorylation status of KaiC, suggesting that KaiB acts by antagonizing the interaction between KaiA and KaiC. A KaiA dimer is sufficient to enhance KaiC hexamer phosphorylation.<ref>PMID:12391300</ref> <ref>PMID:12727878</ref> <ref>PMID:12727879</ref> <ref>PMID:9727980</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	~~[[Category: Anacystis nidulans r2]]~~
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: ~~Egli, M~~]]		[[Category: Synechococcus elongatus PCC 7942 = FACHB-805]]
	[[Category: ~~Pattanayek, R~~]]		[[Category: Egli M]]
	[[Category: ~~Homodimer]]~~		[[Category: Pattanayek R]]
	~~[[Category: Kaic]]~~
	~~[[Category: Kaic phosphorylation activator]]~~
	~~[[Category: Protein binding~~]]

OCA at 11:54, 17 July 2019

2019-07-17T11:54:18Z

← Older revision		Revision as of 11:54, 17 July 2019
Line 1:		Line 1:

	==Crystal structure of the redox-active cofactor DBMIB bound to the full length circadian clock protein KaiA from Synechococcus elongatus==		==Crystal structure of the redox-active cofactor DBMIB bound to the full length circadian clock protein KaiA from Synechococcus elongatus==
	<StructureSection load='4g86' size='340' side='right' caption='[[4g86]], [[Resolution\|resolution]] 2.39Å' scene=''>		<StructureSection load='4g86' size='340' side='right'caption='[[4g86]], [[Resolution\|resolution]] 2.39Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4g86]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Anacystis_nidulans_r2 Anacystis nidulans r2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G86 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G86 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4g86]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Anacystis_nidulans_r2 Anacystis nidulans r2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G86 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G86 FirstGlance]. <br>
Line 22:		Line 22:

	==See Also==		==See Also==
	*[[Circadian clock protein\|Circadian clock protein]]		*[[Circadian clock protein 3D structures\|Circadian clock protein 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 28:		Line 28:
	</StructureSection>		</StructureSection>
	[[Category: Anacystis nidulans r2]]		[[Category: Anacystis nidulans r2]]
			[[Category: Large Structures]]
	[[Category: Egli, M]]		[[Category: Egli, M]]
	[[Category: Pattanayek, R]]		[[Category: Pattanayek, R]]

OCA at 06:11, 5 August 2016

2016-08-05T06:11:29Z

← Older revision		Revision as of 06:11, 5 August 2016
Line 1:		Line 1:

	==Crystal structure of the redox-active cofactor DBMIB bound to the full length circadian clock protein KaiA from Synechococcus elongatus==		==Crystal structure of the redox-active cofactor DBMIB bound to the full length circadian clock protein KaiA from Synechococcus elongatus==
	<StructureSection load='4g86' size='340' side='right' caption='[[4g86]], [[Resolution\|resolution]] 2.39Å' scene=''>		<StructureSection load='4g86' size='340' side='right' caption='[[4g86]], [[Resolution\|resolution]] 2.39Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4g86]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Synechococcus_elongatus_pcc_7942 Synechococcus elongatus pcc 7942~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G86 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G86 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4g86]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Anacystis_nidulans_r2 Anacystis nidulans r2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G86 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G86 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=2PE:NONAETHYLENE+GLYCOL'>2PE</scene>, <scene name='pdbligand=BNT:2,5-DIBROMO-3-ISOPROPYL-6-METHYLBENZO-1,4-QUINONE'>BNT</scene>, <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=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=2PE:NONAETHYLENE+GLYCOL'>2PE</scene>, <scene name='pdbligand=BNT:2,5-DIBROMO-3-ISOPROPYL-6-METHYLBENZO-1,4-QUINONE'>BNT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1r8j\|1r8j]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1r8j\|1r8j]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">kaiA, see0009, Synpcc7942_1218 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1140 ~~Synechococcus elongatus PCC 7942~~])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">kaiA, see0009, Synpcc7942_1218 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1140 Anacystis nidulans R2])</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=4g86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g86 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g86 RCSB], [http://www.ebi.ac.uk/pdbsum/4g86 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=4g86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g86 OCA], [http://pdbe.org/4g86 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4g86 RCSB], [http://www.ebi.ac.uk/pdbsum/4g86 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4g86 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 4g86" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 25:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Synechococcus elongatus pcc 7942~~]]		[[Category: Anacystis nidulans r2]]
	[[Category: Egli, M]]		[[Category: Egli, M]]
	[[Category: Pattanayek, R]]		[[Category: Pattanayek, R]]

OCA at 23:43, 24 December 2014

2014-12-24T23:43:23Z

← Older revision		Revision as of 23:43, 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=4g86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g86 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g86 RCSB], [http://www.ebi.ac.uk/pdbsum/4g86 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=4g86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g86 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g86 RCSB], [http://www.ebi.ac.uk/pdbsum/4g86 PDBsum]</span></td></tr>
	</table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/KAIA_SYNE7 KAIA_SYNE7]] Component of the KaiABC clock protein complex, which constitutes the main circadian regulator in cyanobacteria. The KaiABC complex may act as a promoter-nonspecific transcription regulator that represses transcription, possibly by acting on the state of chromosome compaction. In the complex, it enhances the phosphorylation status of KaiC. In contrast, the presence of KaiB in the complex decreases the phosphorylation status of KaiC, suggesting that KaiB acts by antagonizing the interaction between KaiA and KaiC. A KaiA dimer is sufficient to enhance KaiC hexamer phosphorylation.<ref>PMID:12391300</ref> <ref>PMID:12727878</ref> <ref>PMID:12727879</ref> <ref>PMID:9727980</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 09:30, 10 December 2014

2014-12-10T09:30:17Z

← Older revision		Revision as of 09:30, 10 December 2014
Line 1:		Line 1:
	[[~~Image~~:~~4g86~~.~~png~~\|~~left~~\|~~200px~~]]		==Crystal structure of the redox-active cofactor DBMIB bound to the full length circadian clock protein KaiA from Synechococcus elongatus==
			<StructureSection load='4g86' size='340' side='right' caption='[[4g86]], [[Resolution\|resolution]] 2.39Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[4g86]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Synechococcus_elongatus_pcc_7942 Synechococcus elongatus pcc 7942]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G86 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G86 FirstGlance]. <br>
			</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=2PE:NONAETHYLENE+GLYCOL'>2PE</scene>, <scene name='pdbligand=BNT:2,5-DIBROMO-3-ISOPROPYL-6-METHYLBENZO-1,4-QUINONE'>BNT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
			<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1r8j\|1r8j]]</td></tr>
			<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">kaiA, see0009, Synpcc7942_1218 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1140 Synechococcus elongatus PCC 7942])</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=4g86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g86 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g86 RCSB], [http://www.ebi.ac.uk/pdbsum/4g86 PDBsum]</span></td></tr>
			</table>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			KaiA protein that stimulates KaiC phosphorylation in the cyanobacterial circadian clock was recently shown to be destabilized by dibromothymoquinone (DBMIB), thus revealing KaiA as a sensor of the plastoquinone (PQ) redox state and suggesting an indirect control of the clock by light through PQ redox changes. Here we show using X-ray crystallography that several DBMIBs are bound to KaiA dimer. Some binding modes are consistent with oligomerization of N-terminal KaiA pseudoreceiver domains and/or reduced interdomain flexibility. DBMIB bound to the C-terminal KaiA (C-KaiA) domain and limited stimulation of KaiC kinase activity by C-KaiA in the presence of DBMIB demonstrate that the cofactor may weakly inhibit KaiA-KaiC binding.

	~~{{STRUCTURE_4g86\| PDB=4g86 \| SCENE= }}~~		Crystal Structure of the Redox-Active Cofactor Dibromothymoquinone Bound to Circadian Clock Protein KaiA and Structural Basis for Dibromothymoquinone's Ability to Prevent Stimulation of KaiC Phosphorylation by KaiA.,Pattanayek R, Sidiqi SK, Egli M Biochemistry. 2012 Oct 5. PMID:23020633<ref>PMID:23020633</ref>

	~~===Crystal structure~~ of the ~~redox-active cofactor DBMIB bound to the full length circadian clock protein KaiA from Synechococcus elongatus===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>

	~~{{ABSTRACT_PUBMED_23020633}}~~		==See Also==
			*[[Circadian clock protein\|Circadian clock protein]]
	==~~About this Structure~~==		== References ==
	[[~~4g86~~]] ~~is a 2 chain structure with sequence from [http:~~//~~en.wikipedia.org/wiki/Synechococcus_elongatus_pcc_7942 Synechococcus elongatus pcc 7942]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G86 OCA].~~		<references/>
			__TOC__
			</StructureSection>
	[[Category: Synechococcus elongatus pcc 7942]]		[[Category: Synechococcus elongatus pcc 7942]]
	[[Category: Egli, M.]]		[[Category: Egli, M]]
	[[Category: Pattanayek, R.]]		[[Category: Pattanayek, R]]
	[[Category: Homodimer]]		[[Category: Homodimer]]
	[[Category: Kaic]]		[[Category: Kaic]]
	[[Category: Kaic phosphorylation activator]]		[[Category: Kaic phosphorylation activator]]
	[[Category: Protein binding]]		[[Category: Protein binding]]

OCA at 12:54, 6 March 2013

2013-03-06T12:54:36Z

← Older revision		Revision as of 12:54, 6 March 2013
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	[[Image:4g86.~~jpg~~\|left\|200px]]		[[Image:4g86.png\|left\|200px]]

	{{STRUCTURE_4g86\| PDB=4g86 \| SCENE= }}		{{STRUCTURE_4g86\| PDB=4g86 \| SCENE= }}

OCA at 07:39, 24 October 2012

2012-10-24T07:39:51Z

← Older revision		Revision as of 07:39, 24 October 2012
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	~~'''Unreleased structure'''~~		[[Image:4g86.jpg\|left\|200px]]

	~~The entry~~ 4g86 ~~is ON HOLD~~ ~~until Paper Publication~~		{{STRUCTURE_4g86\| PDB=4g86 \| SCENE= }}

	~~Authors: Pattanayek, R., Egli, M.~~		===Crystal structure of the redox-active cofactor DBMIB bound to the full length circadian clock protein KaiA from Synechococcus elongatus===

	~~Description~~: ~~Crystal structure of the redox~~-~~active cofactor DBMIB bound to the full length circadian clock protein KaiA from~~ Synechococcus elongatus		{{ABSTRACT_PUBMED_23020633}}

			==About this Structure==
			[[4g86]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Synechococcus_elongatus_pcc_7942 Synechococcus elongatus pcc 7942]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G86 OCA].
			[[Category: Synechococcus elongatus pcc 7942]]
			[[Category: Egli, M.]]
			[[Category: Pattanayek, R.]]
			[[Category: Homodimer]]
			[[Category: Kaic]]
			[[Category: Kaic phosphorylation activator]]
			[[Category: Protein binding]]

OCA at 04:51, 5 September 2012

2012-09-05T04:51:19Z

← Older revision		Revision as of 04:51, 5 September 2012
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	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 4g86 is ON HOLD		The entry 4g86 is ON HOLD until Paper Publication

	Authors: Pattanayek, R., Egli, M.		Authors: Pattanayek, R., Egli, M.

	Description: Crystal structure of the redox-active cofactor DBMIB bound to the full length circadian clock protein KaiA from Synechococcus elongatus		Description: Crystal structure of the redox-active cofactor DBMIB bound to the full length circadian clock protein KaiA from Synechococcus elongatus

OCA: Protected "4g86" [edit=sysop:move=sysop]

2012-08-01T05:30:21Z

Protected "4g86" [edit=sysop:move=sysop]

← Older revision	Revision as of 05:30, 1 August 2012
(No difference)