5n8y

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m (Protected "5n8y" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5n8y is ON HOLD
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==KaiCBA circadian clock backbone model based on a Cryo-EM density==
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<StructureSection load='5n8y' size='340' side='right' caption='[[5n8y]], [[Resolution|resolution]] 4.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5n8y]] is a 24 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N8Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5N8Y FirstGlance]. <br>
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</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>
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<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=5n8y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n8y OCA], [http://pdbe.org/5n8y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n8y RCSB], [http://www.ebi.ac.uk/pdbsum/5n8y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n8y ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://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> [[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> [[http://www.uniprot.org/uniprot/KAIB_SYNE7 KAIB_SYNE7]] 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 need the presence of both KaiA and KaiC, suggesting that it acts by antagonizing the interaction between KaiA and KaiC.<ref>PMID:9727980</ref> <ref>PMID:12727878</ref> <ref>PMID:12727879</ref> <ref>PMID:14709675</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Cyanobacteria have a robust circadian oscillator, known as the Kai system. Reconstituted from the purified protein components KaiC, KaiB, and KaiA, it can tick autonomously in the presence of adenosine 5'-triphosphate (ATP). The KaiC hexamers enter a natural 24-hour reaction cycle of autophosphorylation and assembly with KaiB and KaiA in numerous diverse forms. We describe the preparation of stoichiometrically well-defined assemblies of KaiCB and KaiCBA, as monitored by native mass spectrometry, allowing for a structural characterization by single-particle cryo-electron microscopy and mass spectrometry. Our data reveal details of the interactions between the Kai proteins and provide a structural basis to understand periodic assembly of the protein oscillator.
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Authors: Schuller, J.M., Snijder, J., Loessl, P., Heck, A.J.R., Foerster, F.
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Structures of the cyanobacterial circadian oscillator frozen in a fully assembled state.,Snijder J, Schuller JM, Wiegard A, Lossl P, Schmelling N, Axmann IM, Plitzko JM, Forster F, Heck AJ Science. 2017 Mar 17;355(6330):1181-1184. doi: 10.1126/science.aag3218. Epub 2017, Mar 16. PMID:28302852<ref>PMID:28302852</ref>
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Description: KaiCBA circadian clock backbone model based on a Cryo-EM density
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Snijder, J]]
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<div class="pdbe-citations 5n8y" style="background-color:#fffaf0;"></div>
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[[Category: Heck, A.J.R]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Non-specific serine/threonine protein kinase]]
[[Category: Foerster, F]]
[[Category: Foerster, F]]
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[[Category: Heck, A J.R]]
[[Category: Loessl, P]]
[[Category: Loessl, P]]
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[[Category: Schuller, J.M]]
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[[Category: Schuller, J M]]
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[[Category: Snijder, J]]
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[[Category: Aaa+-atpase]]
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[[Category: Circadian clock complex]]
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[[Category: Cyanobacteria]]
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[[Category: Fold-switch]]
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[[Category: Kinase]]
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[[Category: Transferase]]

Revision as of 13:47, 29 March 2017

KaiCBA circadian clock backbone model based on a Cryo-EM density

5n8y, resolution 4.70Å

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