1suy: Difference between revisions
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==NMR structure of the ThKaiA180C-CIIABD complex (average minimized structure)== | |||
<StructureSection load='1suy' size='340' side='right'caption='[[1suy]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1suy]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermosynechococcus_vestitus_BP-1 Thermosynechococcus vestitus BP-1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SUY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SUY FirstGlance]. <br> | |||
</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=1suy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1suy OCA], [https://pdbe.org/1suy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1suy RCSB], [https://www.ebi.ac.uk/pdbsum/1suy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1suy ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/KAIA_THEVB KAIA_THEVB] Key component of the KaiABC oscillator complex, which constitutes the main circadian regulator in cyanobacteria. Complex composition changes during the circadian cycle to control KaiC phosphorylation. KaiA stimulates KaiC autophosphorylation, while KaiB sequesters KaiA, leading to KaiC autodephosphorylation. KaiA binding to the KaiC CII domain during the subjective day yields KaiA(2-4):KaiC(6) complexes which stimulate KaiC autophosphorylation. Phospho-Ser-431 KaiC accumulation triggers binding of KaiB during the subjective night to form the KaiB(6):KaiC(6) complex, leading to changes in the output regulators CikA and SasA. KaiB(6):KaiC(6) formation exposes a site for KaiA binding on KaiB that sequesters KaiA from KaiC's CII domain, making the KaiC(6):KaiB(6):KaiA(12) complex resulting in KaiC autodephosphorylation. Complete dephosphorylation of KaiC leads to dissociation of KaiA(2):KaiB(1), completing 1 cycle of the Kai oscillator (By similarity). Formation of the KaiB:KaiC complex is promoted by KaiA, helping switch KaiC from its autophosphorylation to autodephosphatase function (PubMed:24112939).[UniProtKB:Q79PF6]<ref>PMID:24112939</ref> Binds oxidized quinones via the N-terminal PsR domain, allowing it to sense redox changes and possibly mediate clock input.[UniProtKB:Q79PF6] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/su/1suy_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</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/main_output.php?pdb_ID=1suy ConSurf]. | |||
<div style="clear:both"></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: LiWang AC]] | ||
[[Category: | [[Category: Vakonakis I]] | ||
[[Category: | |||
[[Category: | |||
[[Category: | |||
Latest revision as of 11:35, 1 May 2024
NMR structure of the ThKaiA180C-CIIABD complex (average minimized structure)NMR structure of the ThKaiA180C-CIIABD complex (average minimized structure)
Structural highlights
FunctionKAIA_THEVB Key component of the KaiABC oscillator complex, which constitutes the main circadian regulator in cyanobacteria. Complex composition changes during the circadian cycle to control KaiC phosphorylation. KaiA stimulates KaiC autophosphorylation, while KaiB sequesters KaiA, leading to KaiC autodephosphorylation. KaiA binding to the KaiC CII domain during the subjective day yields KaiA(2-4):KaiC(6) complexes which stimulate KaiC autophosphorylation. Phospho-Ser-431 KaiC accumulation triggers binding of KaiB during the subjective night to form the KaiB(6):KaiC(6) complex, leading to changes in the output regulators CikA and SasA. KaiB(6):KaiC(6) formation exposes a site for KaiA binding on KaiB that sequesters KaiA from KaiC's CII domain, making the KaiC(6):KaiB(6):KaiA(12) complex resulting in KaiC autodephosphorylation. Complete dephosphorylation of KaiC leads to dissociation of KaiA(2):KaiB(1), completing 1 cycle of the Kai oscillator (By similarity). Formation of the KaiB:KaiC complex is promoted by KaiA, helping switch KaiC from its autophosphorylation to autodephosphatase function (PubMed:24112939).[UniProtKB:Q79PF6][1] Binds oxidized quinones via the N-terminal PsR domain, allowing it to sense redox changes and possibly mediate clock input.[UniProtKB:Q79PF6] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See AlsoReferences
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