7dyk: Difference between revisions
New page: '''Unreleased structure''' The entry 7dyk is ON HOLD Authors: Mukaiyama, A., Furuike, Y., Abe, J., Akiyama, S. Description: Crystal Structure of N-terminal C1 domain of KaiC [[Category... |
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The | ==Crystal Structure of Cyanobacterial Circadian Clock Protein KaiC== | ||
<StructureSection load='7dyk' size='340' side='right'caption='[[7dyk]], [[Resolution|resolution]] 2.99Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7dyk]] 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=7DYK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DYK FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.99Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=7dyk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dyk OCA], [https://pdbe.org/7dyk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dyk RCSB], [https://www.ebi.ac.uk/pdbsum/7dyk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dyk ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/KAIC_SYNE7 KAIC_SYNE7] Core component of the KaiABC clock protein complex, which constitutes the main circadian regulator in cyanobacteria. Binds to DNA. The KaiABC complex may act as a promoter-nonspecific transcription regulator that represses transcription, possibly by acting on the state of chromosome compaction.<ref>PMID:9727980</ref> <ref>PMID:14709675</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Spatiotemporal allostery is the source of complex but ordered biological phenomena. To identify the structural basis for allostery that drives the cyanobacterial circadian clock, we crystallized the clock protein KaiC in four distinct states, which cover a whole cycle of phosphor-transfer events at Ser(431) and Thr(432). The minimal set of allosteric events required for oscillatory nature is a bidirectional coupling between the coil-to-helix transition of the Ser(431)-dependent phospho-switch in the C-terminal domain of KaiC and adenosine 5'-diphosphate release from its N-terminal domain during adenosine triphosphatase cycle. An engineered KaiC protein oscillator consisting of a minimal set of the identified master allosteric events exhibited a monophosphorylation cycle of Ser(431) with a temperature-compensated circadian period, providing design principles for simple posttranslational biochemical circadian oscillators. | |||
Elucidation of master allostery essential for circadian clock oscillation in cyanobacteria.,Furuike Y, Mukaiyama A, Ouyang D, Ito-Miwa K, Simon D, Yamashita E, Kondo T, Akiyama S Sci Adv. 2022 Apr 15;8(15):eabm8990. doi: 10.1126/sciadv.abm8990. Epub 2022 Apr, 15. PMID:35427168<ref>PMID:35427168</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[ | </div> | ||
[[Category: | <div class="pdbe-citations 7dyk" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: Akiyama | ==See Also== | ||
[[Category: Furuike | *[[Circadian clock protein 3D structures|Circadian clock protein 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Synechococcus elongatus PCC 7942 = FACHB-805]] | |||
[[Category: Akiyama S]] | |||
[[Category: Furuike Y]] | |||
Latest revision as of 19:43, 29 November 2023
Crystal Structure of Cyanobacterial Circadian Clock Protein KaiCCrystal Structure of Cyanobacterial Circadian Clock Protein KaiC
Structural highlights
FunctionKAIC_SYNE7 Core component of the KaiABC clock protein complex, which constitutes the main circadian regulator in cyanobacteria. Binds to DNA. The KaiABC complex may act as a promoter-nonspecific transcription regulator that represses transcription, possibly by acting on the state of chromosome compaction.[1] [2] Publication Abstract from PubMedSpatiotemporal allostery is the source of complex but ordered biological phenomena. To identify the structural basis for allostery that drives the cyanobacterial circadian clock, we crystallized the clock protein KaiC in four distinct states, which cover a whole cycle of phosphor-transfer events at Ser(431) and Thr(432). The minimal set of allosteric events required for oscillatory nature is a bidirectional coupling between the coil-to-helix transition of the Ser(431)-dependent phospho-switch in the C-terminal domain of KaiC and adenosine 5'-diphosphate release from its N-terminal domain during adenosine triphosphatase cycle. An engineered KaiC protein oscillator consisting of a minimal set of the identified master allosteric events exhibited a monophosphorylation cycle of Ser(431) with a temperature-compensated circadian period, providing design principles for simple posttranslational biochemical circadian oscillators. Elucidation of master allostery essential for circadian clock oscillation in cyanobacteria.,Furuike Y, Mukaiyama A, Ouyang D, Ito-Miwa K, Simon D, Yamashita E, Kondo T, Akiyama S Sci Adv. 2022 Apr 15;8(15):eabm8990. doi: 10.1126/sciadv.abm8990. Epub 2022 Apr, 15. PMID:35427168[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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