4g86
From Proteopedia
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| - | [[ | + | ==Crystal structure of the redox-active cofactor DBMIB bound to the full length circadian clock protein KaiA from Synechococcus elongatus== |
| + | <StructureSection load='4g86' size='340' side='right' caption='[[4g86]], [[Resolution|resolution]] 2.39Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4g86]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Synechococcus_elongatus_pcc_7942 Synechococcus elongatus pcc 7942]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G86 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G86 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=2PE:NONAETHYLENE+GLYCOL'>2PE</scene>, <scene name='pdbligand=BNT:2,5-DIBROMO-3-ISOPROPYL-6-METHYLBENZO-1,4-QUINONE'>BNT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1r8j|1r8j]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">kaiA, see0009, Synpcc7942_1218 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1140 Synechococcus elongatus PCC 7942])</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4g86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g86 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g86 RCSB], [http://www.ebi.ac.uk/pdbsum/4g86 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | KaiA protein that stimulates KaiC phosphorylation in the cyanobacterial circadian clock was recently shown to be destabilized by dibromothymoquinone (DBMIB), thus revealing KaiA as a sensor of the plastoquinone (PQ) redox state and suggesting an indirect control of the clock by light through PQ redox changes. Here we show using X-ray crystallography that several DBMIBs are bound to KaiA dimer. Some binding modes are consistent with oligomerization of N-terminal KaiA pseudoreceiver domains and/or reduced interdomain flexibility. DBMIB bound to the C-terminal KaiA (C-KaiA) domain and limited stimulation of KaiC kinase activity by C-KaiA in the presence of DBMIB demonstrate that the cofactor may weakly inhibit KaiA-KaiC binding. | ||
| - | + | Crystal Structure of the Redox-Active Cofactor Dibromothymoquinone Bound to Circadian Clock Protein KaiA and Structural Basis for Dibromothymoquinone's Ability to Prevent Stimulation of KaiC Phosphorylation by KaiA.,Pattanayek R, Sidiqi SK, Egli M Biochemistry. 2012 Oct 5. PMID:23020633<ref>PMID:23020633</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| - | + | ==See Also== | |
| - | + | *[[Circadian clock protein|Circadian clock protein]] | |
| - | == | + | == References == |
| - | [[ | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Synechococcus elongatus pcc 7942]] | [[Category: Synechococcus elongatus pcc 7942]] | ||
| - | [[Category: Egli, M | + | [[Category: Egli, M]] |
| - | [[Category: Pattanayek, R | + | [[Category: Pattanayek, R]] |
[[Category: Homodimer]] | [[Category: Homodimer]] | ||
[[Category: Kaic]] | [[Category: Kaic]] | ||
[[Category: Kaic phosphorylation activator]] | [[Category: Kaic phosphorylation activator]] | ||
[[Category: Protein binding]] | [[Category: Protein binding]] | ||
Revision as of 09:30, 10 December 2014
Crystal structure of the redox-active cofactor DBMIB bound to the full length circadian clock protein KaiA from Synechococcus elongatus
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