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7dye

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Crystal Structure of Cyanobacterial Circadian Clock Protein KaiC

Structural highlights

7dye is a 2 chain structure with sequence from Synechococcus elongatus PCC 7942 = FACHB-805. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.6Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1] ^[2]

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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
↑ Nakahira Y, Katayama M, Miyashita H, Kutsuna S, Iwasaki H, Oyama T, Kondo T. Global gene repression by KaiC as a master process of prokaryotic circadian system. Proc Natl Acad Sci U S A. 2004 Jan 20;101(3):881-5. Epub 2004 Jan 6. PMID:14709675 doi:10.1073/pnas.0307411100
↑ 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. Regulation mechanisms of the dual ATPase in KaiC. Proc Natl Acad Sci U S A. 2022 May 10;119(19):e2119627119. PMID:35507871 doi:10.1073/pnas.2119627119

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7dye"

Categories: Large Structures | Synechococcus elongatus PCC 7942 = FACHB-805 | Akiyama S | Furuike Y

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 7dye is ON HOLD
+==Crystal Structure of Cyanobacterial Circadian Clock Protein KaiC==
+<StructureSection load='7dye' size='340' side='right'caption='[[7dye]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7dye]] 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=7DYE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DYE 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]] 2.6&#8491;</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=7dye FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dye OCA], [https://pdbe.org/7dye PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dye RCSB], [https://www.ebi.ac.uk/pdbsum/7dye PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dye 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 ==
+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.
-Authors: Mukaiyama, A., Furuike, Y., Abe, J., Akiyama, S.
+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>
-Description: Crystal Structure of N-terminal C1 domain of KaiC
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Abe, J]]
+<div class="pdbe-citations 7dye" style="background-color:#fffaf0;"></div>
-[[Category: Mukaiyama, A]]
-[[Category: Akiyama, S]]
+==See Also==
-[[Category: Furuike, Y]]
+*[[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]]

7dye

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Current revision

Crystal Structure of Cyanobacterial Circadian Clock Protein KaiC

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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