7dy1: Difference between revisions
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==Crystal Structure of Cyanobacterial Circadian Clock Protein KaiC== | |||
<StructureSection load='7dy1' size='340' side='right'caption='[[7dy1]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7dy1]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermosynechococcus_vestitus_BP-1 Thermosynechococcus vestitus BP-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DY1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DY1 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]] 2.2Å</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>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</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=7dy1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dy1 OCA], [https://pdbe.org/7dy1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dy1 RCSB], [https://www.ebi.ac.uk/pdbsum/7dy1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dy1 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/KAIC_THEVB KAIC_THEVB] 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 (By similarity). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
SignificanceKaiC, a core clock protein in the cyanobacterial circadian clock system, hydrolyzes adenosine triphosphate (ATP) at two distinct sites in a slow but ordered manner to measure the circadian timescale. We used biochemical and structural biology techniques to characterize the properties and interplay of dual-adenosine triphosphatase (ATPase) active sites. Our results show that the N-terminal and C-terminal ATPases communicate with each other through an interface between the N-terminal and C-terminal domains in KaiC. The dual-ATPase sites are regulated rhythmically in a concerted or opposing manner dependent on the phase of the circadian clock system, controlling the affinities of KaiC for other clock proteins, KaiA and KaiB. | |||
Regulation mechanisms of the dual ATPase in KaiC.,Furuike Y, Mukaiyama A, Koda SI, Simon D, Ouyang D, Ito-Miwa K, Saito S, Yamashita E, Nishiwaki-Ohkawa T, Terauchi K, Kondo T, Akiyama S Proc Natl Acad Sci U S A. 2022 May 10;119(19):e2119627119. doi:, 10.1073/pnas.2119627119. Epub 2022 May 4. PMID:35507871<ref>PMID:35507871</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7dy1" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Circadian clock protein 3D structures|Circadian clock protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Thermosynechococcus vestitus BP-1]] | |||
[[Category: Akiyama S]] | |||
[[Category: Furuike Y]] | |||
