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| | ==NMR structure of foldswitch-stablized KaiB in complex with pseudo receiver domain of CikA from Thermosynechococcus elongatus== | | ==NMR structure of foldswitch-stablized KaiB in complex with pseudo receiver domain of CikA from Thermosynechococcus elongatus== |
| - | <StructureSection load='5jyv' size='340' side='right'caption='[[5jyv]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='5jyv' size='340' side='right'caption='[[5jyv]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5jyv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Theeb Theeb]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JYV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JYV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5jyv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermosynechococcus_vestitus_BP-1 Thermosynechococcus vestitus BP-1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JYV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JYV FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5jyu|5jyu]], [[5jyt|5jyt]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tll0899 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=197221 THEEB]), kaiB, tlr0482 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=197221 THEEB])</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=5jyv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jyv OCA], [https://pdbe.org/5jyv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jyv RCSB], [https://www.ebi.ac.uk/pdbsum/5jyv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jyv 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=5jyv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jyv OCA], [http://pdbe.org/5jyv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jyv RCSB], [http://www.ebi.ac.uk/pdbsum/5jyv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jyv ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/KAIB_THEEB KAIB_THEEB]] Component of the KaiABC clock protein complex, which constitutes the main circadian regulator in cyanobacteria. The KaiABC complex may act as a promoter-non-specific transcription regulator that represses transcription, possibly by acting on the state of chromosome compaction. In the complex, it decreases the phosphorylation status of KaiC. It has no effect on KaiC by itself, but instead needs the presence of both KaiA and KaiC, suggesting that it acts by antagonizing the interaction between KaiA and KaiC.[HAMAP-Rule:MF_01835] | + | [https://www.uniprot.org/uniprot/Q8DKG0_THEVB Q8DKG0_THEVB] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Theeb]] | + | [[Category: Thermosynechococcus vestitus BP-1]] |
| - | [[Category: LiWang, A L]] | + | [[Category: LiWang AL]] |
| - | [[Category: Tseng, R D]] | + | [[Category: Tseng RD]] |
| - | [[Category: Circadian clock]]
| + | |
| - | [[Category: Sigaling protein]]
| + | |
| - | [[Category: Signaling protein complex]]
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| Structural highlights
Function
Q8DKG0_THEVB
Publication Abstract from PubMed
Circadian clocks are ubiquitous timing systems that induce rhythms of biological activities in synchrony with night and day. In cyanobacteria, timing is generated by a posttranslational clock consisting of KaiA, KaiB, and KaiC proteins and a set of output signaling proteins, SasA and CikA, which transduce this rhythm to control gene expression. Here, we describe crystal and nuclear magnetic resonance structures of KaiB-KaiC,KaiA-KaiB-KaiC, and CikA-KaiB complexes. They reveal how the metamorphic properties of KaiB, a protein that adopts two distinct folds, and the post-adenosine triphosphate hydrolysis state of KaiC create a hub around which nighttime signaling events revolve, including inactivation of KaiA and reciprocal regulation of the mutually antagonistic signaling proteins, SasA and CikA.
Structural basis of the day-night transition in a bacterial circadian clock.,Tseng R, Goularte NF, Chavan A, Luu J, Cohen SE, Chang YG, Heisler J, Li S, Michael AK, Tripathi S, Golden SS, LiWang A, Partch CL Science. 2017 Mar 17;355(6330):1174-1180. doi: 10.1126/science.aag2516. Epub 2017, Mar 16. PMID:28302851[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tseng R, Goularte NF, Chavan A, Luu J, Cohen SE, Chang YG, Heisler J, Li S, Michael AK, Tripathi S, Golden SS, LiWang A, Partch CL. Structural basis of the day-night transition in a bacterial circadian clock. Science. 2017 Mar 17;355(6330):1174-1180. doi: 10.1126/science.aag2516. Epub 2017, Mar 16. PMID:28302851 doi:http://dx.doi.org/10.1126/science.aag2516
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