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| | ==Crystal structure of the phosphorylation-site double mutant S431E/T432E of the KaiC circadian clock protein== | | ==Crystal structure of the phosphorylation-site double mutant S431E/T432E of the KaiC circadian clock protein== |
| - | <StructureSection load='3s1a' size='340' side='right' caption='[[3s1a]], [[Resolution|resolution]] 3.00Å' scene=''> | + | <StructureSection load='3s1a' size='340' side='right'caption='[[3s1a]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3s1a]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Synechococcus_elongatus Synechococcus elongatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S1A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3S1A FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3s1a]] 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]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S1A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S1A FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><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]] 3Å</td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></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></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3dvl|3dvl]], [[3k0c|3k0c]], [[3k0f|3k0f]]</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=3s1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s1a OCA], [https://pdbe.org/3s1a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s1a RCSB], [https://www.ebi.ac.uk/pdbsum/3s1a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s1a ProSAT]</span></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">kaiC, see0011, Synpcc7942_1216 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=32046 Synechococcus elongatus])</td></tr>
| + | </table> |
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr> | + | == Function == |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3s1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s1a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3s1a RCSB], [http://www.ebi.ac.uk/pdbsum/3s1a PDBsum]</span></td></tr> | + | [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> |
| - | <table> | + | |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | Combined SAXS/EM Based Models of the S. elongatus Post-Translational Circadian Oscillator and its Interactions with the Output His-Kinase SasA.,Pattanayek R, Williams DR, Rossi G, Weigand S, Mori T, Johnson CH, Stewart PL, Egli M PLoS One. 2011;6(8):e23697. Epub 2011 Aug 24. PMID:21887298<ref>PMID:21887298</ref> | | Combined SAXS/EM Based Models of the S. elongatus Post-Translational Circadian Oscillator and its Interactions with the Output His-Kinase SasA.,Pattanayek R, Williams DR, Rossi G, Weigand S, Mori T, Johnson CH, Stewart PL, Egli M PLoS One. 2011;6(8):e23697. Epub 2011 Aug 24. PMID:21887298<ref>PMID:21887298</ref> |
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 3s1a" style="background-color:#fffaf0;"></div> |
| | | | |
| | ==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: Non-specific serine/threonine protein kinase]] | + | [[Category: Large Structures]] |
| - | [[Category: Synechococcus elongatus]] | + | [[Category: Synechococcus elongatus PCC 7942 = FACHB-805]] |
| - | [[Category: Egli, M.]] | + | [[Category: Egli M]] |
| - | [[Category: Johnson, C H.]] | + | [[Category: Johnson CH]] |
| - | [[Category: Mori, T.]] | + | [[Category: Mori T]] |
| - | [[Category: Pattanayek, R.]] | + | [[Category: Pattanayek R]] |
| - | [[Category: Rossi, G.]] | + | [[Category: Rossi G]] |
| - | [[Category: Stewart, P L.]] | + | [[Category: Stewart PL]] |
| - | [[Category: Weigand, S.]] | + | [[Category: Weigand S]] |
| - | [[Category: Williams, D W.]] | + | [[Category: Williams DW]] |
| - | [[Category: Atp binding]]
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| - | [[Category: Auto-kinase]]
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| - | [[Category: Hexamer]]
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| - | [[Category: Mg binding]]
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| - | [[Category: Phophatase]]
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| - | [[Category: Phosphorylation]]
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| - | [[Category: Serine threonine kinase]]
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| - | [[Category: Transferase]]
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| Structural highlights
Function
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.[1] [2]
Publication Abstract from PubMed
The circadian clock in the cyanobacterium Synechococcus elongatus is composed of a post-translational oscillator (PTO) that can be reconstituted in vitro from three different proteins in the presence of ATP and a transcription-translation feedback loop (TTFL). The homo-hexameric KaiC kinase, phosphatase and ATPase alternates between hypo- and hyper-phosphorylated states over the 24-h cycle, with KaiA enhancing phosphorylation, and KaiB antagonizing KaiA and promoting KaiC subunit exchange. SasA is a His kinase that relays output signals from the PTO formed by the three Kai proteins to the TTFL. Although the crystal structures for all three Kai proteins are known, atomic resolution structures of Kai and Kai/SasA protein complexes have remained elusive. Here, we present models of the KaiAC and KaiBC complexes derived from solution small angle X-ray scattering (SAXS), which are consistent with previous EM based models. We also present a combined SAXS/EM model of the KaiC/SasA complex, which has two N-terminal SasA sensory domains occupying positions on the C-terminal KaiC ring reminiscent of the orientations adopted by KaiB dimers. Using EM we demonstrate that KaiB and SasA compete for similar binding sites on KaiC. We also propose an EM based model of the ternary KaiABC complex that is consistent with the sequestering of KaiA by KaiB on KaiC during the PTO dephosphorylation phase. This work provides the first 3D-catalogue of protein-protein interactions in the KaiABC PTO and the output pathway mediated by SasA.
Combined SAXS/EM Based Models of the S. elongatus Post-Translational Circadian Oscillator and its Interactions with the Output His-Kinase SasA.,Pattanayek R, Williams DR, Rossi G, Weigand S, Mori T, Johnson CH, Stewart PL, Egli M PLoS One. 2011;6(8):e23697. Epub 2011 Aug 24. PMID:21887298[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ishiura M, Kutsuna S, Aoki S, Iwasaki H, Andersson CR, Tanabe A, Golden SS, Johnson CH, Kondo T. Expression of a gene cluster kaiABC as a circadian feedback process in cyanobacteria. Science. 1998 Sep 4;281(5382):1519-23. PMID:9727980
- ↑ Nakahira Y, Katayama M, Miyashita H, Kutsuna S, Iwasaki H, Oyama T, Kondo T. Global gene repression by KaiC as a master process of prokaryotic circadian system. Proc Natl Acad Sci U S A. 2004 Jan 20;101(3):881-5. Epub 2004 Jan 6. PMID:14709675 doi:10.1073/pnas.0307411100
- ↑ Pattanayek R, Williams DR, Rossi G, Weigand S, Mori T, Johnson CH, Stewart PL, Egli M. Combined SAXS/EM Based Models of the S. elongatus Post-Translational Circadian Oscillator and its Interactions with the Output His-Kinase SasA. PLoS One. 2011;6(8):e23697. Epub 2011 Aug 24. PMID:21887298 doi:10.1371/journal.pone.0023697
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