2j48
From Proteopedia
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- | [[Image:2j48.jpg|left|200px]] | ||
- | + | ==NMR structure of the pseudo-receiver domain of the CikA protein.== | |
- | + | <StructureSection load='2j48' size='340' side='right'caption='[[2j48]]' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[2j48]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_elongatus_PCC_7942_=_FACHB-805 Synechococcus elongatus PCC 7942 = FACHB-805]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J48 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J48 FirstGlance]. <br> | |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2j48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j48 OCA], [https://pdbe.org/2j48 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j48 RCSB], [https://www.ebi.ac.uk/pdbsum/2j48 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j48 ProSAT]</span></td></tr> | |
- | + | </table> | |
- | | | + | == Function == |
- | + | [https://www.uniprot.org/uniprot/Q9KHI5_SYNE7 Q9KHI5_SYNE7] | |
- | + | == 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/j4/2j48_consurf.spt"</scriptWhenChecked> | |
- | == | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2j48 ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
The circadian input kinase (CikA) is a major element of the pathway that provides environmental information to the circadian clock of the cyanobacterium Synechococcus elongatus. CikA is a polypeptide of 754 residues and has three recognizable domains: GAF, histidine protein kinase, and receiver-like. This latter domain of CikA lacks the conserved phospho-accepting aspartyl residue of bona fide receiver domains and is thus a pseudo-receiver (PsR). Recently, it was shown that the PsR domain (1) attenuates the autokinase activity of CikA, (2) is necessary to localize CikA to the cell pole, and (3) is necessary for the destabilization of CikA in the presence of the quinone analog 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone (DBMIB). The solution structure of the PsR domain of CikA, CikAPsR, is presented here. A model of the interaction between the PsR domain and HPK portion of CikA provides a potential explanation for how the PsR domain attenuates the autokinase activity of CikA. Finally, a likely quinone-binding surface on CikAPsR is shown here. | The circadian input kinase (CikA) is a major element of the pathway that provides environmental information to the circadian clock of the cyanobacterium Synechococcus elongatus. CikA is a polypeptide of 754 residues and has three recognizable domains: GAF, histidine protein kinase, and receiver-like. This latter domain of CikA lacks the conserved phospho-accepting aspartyl residue of bona fide receiver domains and is thus a pseudo-receiver (PsR). Recently, it was shown that the PsR domain (1) attenuates the autokinase activity of CikA, (2) is necessary to localize CikA to the cell pole, and (3) is necessary for the destabilization of CikA in the presence of the quinone analog 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone (DBMIB). The solution structure of the PsR domain of CikA, CikAPsR, is presented here. A model of the interaction between the PsR domain and HPK portion of CikA provides a potential explanation for how the PsR domain attenuates the autokinase activity of CikA. Finally, a likely quinone-binding surface on CikAPsR is shown here. | ||
- | + | NMR structure of the pseudo-receiver domain of CikA.,Gao T, Zhang X, Ivleva NB, Golden SS, LiWang A Protein Sci. 2007 Mar;16(3):465-75. PMID:17322531<ref>PMID:17322531</ref> | |
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- | NMR structure of the pseudo-receiver domain of CikA., Gao T, Zhang X, Ivleva NB, Golden SS, LiWang A | + | |
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- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
+ | </div> | ||
+ | <div class="pdbe-citations 2j48" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Synechococcus elongatus PCC 7942 = FACHB-805]] | ||
+ | [[Category: Gao T]] | ||
+ | [[Category: Golden SS]] | ||
+ | [[Category: LiWang A]] | ||
+ | [[Category: Zhang X]] |
Current revision
NMR structure of the pseudo-receiver domain of the CikA protein.
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