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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]]
| + | |
| Structural highlights
Function
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.[1] [2] [3] [4]
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[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Iwasaki H, Nishiwaki T, Kitayama Y, Nakajima M, Kondo T. KaiA-stimulated KaiC phosphorylation in circadian timing loops in cyanobacteria. Proc Natl Acad Sci U S A. 2002 Nov 26;99(24):15788-93. Epub 2002 Oct 21. PMID:12391300 doi:http://dx.doi.org/10.1073/pnas.222467299
- ↑ Xu Y, Mori T, Johnson CH. Cyanobacterial circadian clockwork: roles of KaiA, KaiB and the kaiBC promoter in regulating KaiC. EMBO J. 2003 May 1;22(9):2117-26. PMID:12727878 doi:10.1093/emboj/cdg168
- ↑ Kitayama Y, Iwasaki H, Nishiwaki T, Kondo T. KaiB functions as an attenuator of KaiC phosphorylation in the cyanobacterial circadian clock system. EMBO J. 2003 May 1;22(9):2127-34. PMID:12727879 doi:10.1093/emboj/cdg212
- ↑ Ishiura M, Kutsuna S, Aoki S, Iwasaki H, Andersson CR, Tanabe A, Golden SS, Johnson CH, Kondo T. Expression of a gene cluster kaiABC as a circadian feedback process in cyanobacteria. Science. 1998 Sep 4;281(5382):1519-23. PMID:9727980
- ↑ Pattanayek R, Sidiqi SK, Egli M. 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. Biochemistry. 2012 Oct 5. PMID:23020633 doi:http://dx.doi.org/10.1021/bi301222t
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