1q6a: Difference between revisions

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 ==Solution Structure of the C-terminal Domain of Thermosynechococcus elongatus KaiA (ThKaiA180C); Averaged Minimized Structure==
-<StructureSection load='1q6a' size='340' side='right'caption='[[1q6a]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
+<StructureSection load='1q6a' size='340' side='right'caption='[[1q6a]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1q6a]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Theeb Theeb]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q6A OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1Q6A FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1q6a]] is a 2 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=1Q6A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q6A FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KaiA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=197221 THEEB])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1q6a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q6a OCA], [http://pdbe.org/1q6a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1q6a RCSB], [http://www.ebi.ac.uk/pdbsum/1q6a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1q6a ProSAT]</span></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=1q6a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q6a OCA], [https://pdbe.org/1q6a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q6a RCSB], [https://www.ebi.ac.uk/pdbsum/1q6a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q6a ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/KAIA_THEEB KAIA_THEEB]] 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.
+[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]]
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    <jmolCheckbox>
      <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q6/1q6a_consurf.spt"</scriptWhenChecked>
-     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
    </jmolCheckbox>
@@ Line 36: / Line 36: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Theeb]]
+[[Category: Thermosynechococcus vestitus BP-1]]
-[[Category: Golden, S S]]
+[[Category: Golden SS]]
-[[Category: Holzenburg, A]]
+[[Category: Holzenburg A]]
-[[Category: LiWang, A C]]
+[[Category: LiWang AC]]
-[[Category: Sun, J]]
+[[Category: Sun J]]
-[[Category: Vakonakis, I]]
+[[Category: Vakonakis I]]
-[[Category: All alpha-helix protein]]
-[[Category: Circadian clock protein]]
-[[Category: Homodimer]]