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==Solution structure of the N-terminal domain of Synechococcus elongatus KaiA (KaiA135N); Average minimized structure.== | ==Solution structure of the N-terminal domain of Synechococcus elongatus KaiA (KaiA135N); Average minimized structure.== | ||
<StructureSection load='1m2e' size='340' side='right' caption='[[1m2e | <StructureSection load='1m2e' size='340' side='right'caption='[[1m2e]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1m2e]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1m2e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_elongatus Synechococcus elongatus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M2E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M2E FirstGlance]. <br> | ||
</td></tr><tr id=' | </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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1m2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m2e OCA], [https://pdbe.org/1m2e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m2e RCSB], [https://www.ebi.ac.uk/pdbsum/1m2e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m2e ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://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> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m2/1m2e_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m2/1m2e_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1m2e ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 30: | Line 30: | ||
==See Also== | ==See Also== | ||
*[[Circadian clock protein|Circadian clock protein]] | *[[Circadian clock protein 3D structures|Circadian clock protein 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Synechococcus elongatus]] | ||
[[Category: | [[Category: Golden SS]] | ||
[[Category: | [[Category: LiWang AC]] | ||
[[Category: | [[Category: Vakonakis I]] | ||
[[Category: | [[Category: Williams SB]] | ||
Latest revision as of 11:48, 22 May 2024
Solution structure of the N-terminal domain of Synechococcus elongatus KaiA (KaiA135N); Average minimized structure.Solution structure of the N-terminal domain of Synechococcus elongatus KaiA (KaiA135N); Average minimized structure.
Structural highlights
FunctionKAIA_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.[1] [2] [3] [4] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedIn the cyanobacterium Synechococcus elongatus (PCC 7942) the proteins KaiA, KaiB, and KaiC are required for circadian clock function. We deduced a circadian clock function for KaiA from a combination of biochemical and structural data. Both KaiA and its isolated carboxyl-terminal domain (KaiA180C) stimulated KaiC autophosphorylation and facilitated attenuation of KaiC autophosphorylation by KaiB. An amino-terminal domain (KaiA135N) had no function in the autophosphorylation assay. NMR structure determination showed that KaiA135N is a pseudo-receiver domain. We propose that this pseudo-receiver is a timing input-device that regulates KaiA stimulation of KaiC autophosphorylation, which in turn is essential for circadian timekeeping. Structure and function from the circadian clock protein KaiA of Synechococcus elongatus: a potential clock input mechanism.,Williams SB, Vakonakis I, Golden SS, LiWang AC Proc Natl Acad Sci U S A. 2002 Nov 26;99(24):15357-62. Epub 2002 Nov 15. PMID:12438647[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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