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[[Image:2gbl.gif|left|200px]]
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{{STRUCTURE_2gbl|  PDB=2gbl  |  SCENE=  }}
'''Crystal Structure of Full Length Circadian Clock Protein KaiC with Phosphorylation Sites'''


==Crystal Structure of Full Length Circadian Clock Protein KaiC with Phosphorylation Sites==
<StructureSection load='2gbl' size='340' side='right'caption='[[2gbl]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2gbl]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_elongatus_PCC_7942_=_FACHB-805 Synechococcus elongatus PCC 7942 = FACHB-805]. The January 2008 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Circadian Clock Proteins''  by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2008_1 10.2210/rcsb_pdb/mom_2008_1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GBL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GBL FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#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=2gbl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gbl OCA], [https://pdbe.org/2gbl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gbl RCSB], [https://www.ebi.ac.uk/pdbsum/2gbl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gbl ProSAT]</span></td></tr>
</table>
== Function ==
[https://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>
== 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/gb/2gbl_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2gbl ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The cyanobacterial circadian clock can be reconstituted in vitro by mixing recombinant KaiA, KaiB and KaiC proteins with ATP, producing KaiC phosphorylation and dephosphorylation cycles that have a regular rhythm with a ca. 24-h period and are temperature-compensated. KaiA and KaiB are modulators of KaiC phosphorylation, whereby KaiB antagonizes KaiA's action. Here, we present a complete crystallographic model of the Synechococcus elongatus KaiC hexamer that includes previously unresolved portions of the C-terminal regions, and a negative-stain electron microscopy study of S. elongatus and Thermosynechococcus elongatus BP-1 KaiA-KaiC complexes. Site-directed mutagenesis in combination with EM reveals that KaiA binds exclusively to the CII half of the KaiC hexamer. The EM-based model of the KaiA-KaiC complex reveals protein-protein interactions at two sites: the known interaction of the flexible C-terminal KaiC peptide with KaiA, and a second postulated interaction between the apical region of KaiA and the ATP binding cleft on KaiC. This model brings KaiA mutation sites that alter clock period or abolish rhythmicity into contact with KaiC and suggests how KaiA might regulate KaiC phosphorylation.


==Overview==
Analysis of KaiA-KaiC protein interactions in the cyano-bacterial circadian clock using hybrid structural methods.,Pattanayek R, Williams DR, Pattanayek S, Xu Y, Mori T, Johnson CH, Stewart PL, Egli M EMBO J. 2006 May 3;25(9):2017-28. Epub 2006 Apr 20. PMID:16628225<ref>PMID:16628225</ref>
The cyanobacterial circadian clock can be reconstituted in vitro by mixing recombinant KaiA, KaiB and KaiC proteins with ATP, producing KaiC phosphorylation and dephosphorylation cycles that have a regular rhythm with a ca. 24-h period and are temperature-compensated. KaiA and KaiB are modulators of KaiC phosphorylation, whereby KaiB antagonizes KaiA's action. Here, we present a complete crystallographic model of the Synechococcus elongatus KaiC hexamer that includes previously unresolved portions of the C-terminal regions, and a negative-stain electron microscopy study of S. elongatus and Thermosynechococcus elongatus BP-1 KaiA-KaiC complexes. Site-directed mutagenesis in combination with EM reveals that KaiA binds exclusively to the CII half of the KaiC hexamer. The EM-based model of the KaiA-KaiC complex reveals protein-protein interactions at two sites: the known interaction of the flexible C-terminal KaiC peptide with KaiA, and a second postulated interaction between the apical region of KaiA and the ATP binding cleft on KaiC. This model brings KaiA mutation sites that alter clock period or abolish rhythmicity into contact with KaiC and suggests how KaiA might regulate KaiC phosphorylation.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2GBL is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Synechococcus_sp. Synechococcus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GBL OCA].
</div>
<div class="pdbe-citations 2gbl" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Analysis of KaiA-KaiC protein interactions in the cyano-bacterial circadian clock using hybrid structural methods., Pattanayek R, Williams DR, Pattanayek S, Xu Y, Mori T, Johnson CH, Stewart PL, Egli M, EMBO J. 2006 May 3;25(9):2017-28. Epub 2006 Apr 20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16628225 16628225]
*[[Circadian clock protein 3D structures|Circadian clock protein 3D structures]]
[[Category: Non-specific serine/threonine protein kinase]]
== References ==
[[Category: Protein complex]]
<references/>
[[Category: Synechococcus sp.]]
__TOC__
[[Category: Egli, M.]]
</StructureSection>
[[Category: Johnson, C H.]]
[[Category: Circadian Clock Proteins]]
[[Category: Mori, T.]]
[[Category: Large Structures]]
[[Category: Pattanayek, R.]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Pattanayek, S.]]
[[Category: Synechococcus elongatus PCC 7942 = FACHB-805]]
[[Category: Stewart, P L.]]
[[Category: Egli M]]
[[Category: Williams, D R.]]
[[Category: Johnson CH]]
[[Category: Xu, Y.]]
[[Category: Mori T]]
[[Category: Circadian]]
[[Category: Pattanayek R]]
[[Category: Circadian clock protein homohexamer]]
[[Category: Pattanayek S]]
[[Category: Hexamer]]
[[Category: Stewart PL]]
[[Category: Kaia]]
[[Category: Williams DR]]
[[Category: Kaib]]
[[Category: Xu Y]]
[[Category: Kaic]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 04:55:08 2008''

Latest revision as of 07:38, 9 October 2024

Crystal Structure of Full Length Circadian Clock Protein KaiC with Phosphorylation Sites

2gbl, resolution 2.80Å

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