4o0m

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:21, 30 October 2024) (edit) (undo)
 
Line 4: Line 4:
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4o0m]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermosynechococcus_vestitus_BP-1 Thermosynechococcus vestitus BP-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O0M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O0M FirstGlance]. <br>
<table><tr><td colspan='2'>[[4o0m]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermosynechococcus_vestitus_BP-1 Thermosynechococcus vestitus BP-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O0M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O0M FirstGlance]. <br>
-
</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>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.84&#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>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</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=4o0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o0m OCA], [https://pdbe.org/4o0m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o0m RCSB], [https://www.ebi.ac.uk/pdbsum/4o0m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o0m 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=4o0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o0m OCA], [https://pdbe.org/4o0m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o0m RCSB], [https://www.ebi.ac.uk/pdbsum/4o0m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o0m ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[https://www.uniprot.org/uniprot/KAIC_THEVB KAIC_THEVB] 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 (By similarity).
+
[https://www.uniprot.org/uniprot/KAIC_THEVB KAIC_THEVB] Central 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. Clock output pathways impact the RpaA transcriptional regulator. KaiC enhances the autophosphorylation activity of SasA, which then transfers its phosphate group to RpaA to activate it. KaiB and KaiC together enhance the phospho-RpaA dephosphatase activity of CikA.[HAMAP-Rule:MF_01836] Stimulates SasA autophosphorylation. Fully phosphorylated KaiC (tested with phosphomimetic Asp-431-432-Asp) is the best stimulant, requires the ATPase activity of the CII domain. Unphosphorylated SasA associates with KaiC and its autophosphorylation activity is enhanced. Phospho-SasA is released and associates with RpaA, transferring its phosphate group (PubMed:22512339). Formation of the KaiA:KaiB complex is promoted by KaiC, helping switch KaiC from its autophosphorylation to autodephosphatase function (PubMed:24112939, PubMed:28302851).<ref>PMID:22512339</ref> <ref>PMID:24112939</ref> <ref>PMID:28302851</ref> Has a weak, temperature-independent ATPase activity (about 14 molecules of ATP per day) that defines the circadian period (PubMed:28302851, PubMed:34618577). ATPase activity is mostly contributed by the CI domain; the CII domain augments the activity. The addition of KaiA increases activity. ATPase is inhibited during the KaiC phosphorylating phase and activated during the KaiC dephosphorylating phase (PubMed:35507871).<ref>PMID:28302851</ref> <ref>PMID:34618577</ref> <ref>PMID:35507871</ref>
-
<div style="background-color:#fffaf0;">
+
-
== Publication Abstract from PubMed ==
+
-
A post-translational oscillator (PTO) composed of the proteins KaiA, KaiB and KaiC is at the heart of the cyanobacterial circadian clock. KaiC interacts with KaiA and KaiB over the daily cycle, and CII domains undergo rhythmic phosphorylation/dephosphorylation with a 24 h period. Both the N-terminal (CI) and C-terminal (CII) rings of KaiC exhibit ATPase activity. The CI ATPase proceeds in an input-independent fashion, but the CII ATPase is subject to metabolic input signals. The crystal structure of KaiC from Thermosynechococcus elongatus allows insight into the different anatomies of the CI and CII ATPases. Four consecutive arginines in CI (Arg linker) that connect the P-loop, CI subunits and CI and CII at the ring interface are primary candidates for the coordination of the CI and CII activities. The mutation of linker residues alters the period or triggers arhythmic behavior. Comparison between the CI and CII structures also reveals differences in loop regions that are key to KaiA and KaiB binding and activation of CII ATPase and kinase. Common packing features in KaiC crystals shed light on the KaiB-KaiC interaction.
+
-
 
+
-
An arginine tetrad as mediator of input-dependent and input-independent ATPases in the clock protein KaiC.,Pattanayek R, Xu Y, Lamichhane A, Johnson CH, Egli M Acta Crystallogr D Biol Crystallogr. 2014 May;70(Pt 5):1375-90. doi: , 10.1107/S1399004714003228. Epub 2014 Apr 30. PMID:24816106<ref>PMID:24816106</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 4o0m" style="background-color:#fffaf0;"></div>
+
==See Also==
==See Also==

Current revision

Crystal structure of T. Elongatus BP-1 Clock Protein KaiC

PDB ID 4o0m

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4o0m"
Personal tools