1t4y

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[[Image:1t4y.jpg|left|200px]]<br /><applet load="1t4y" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1t4y" />
 
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'''Solution structure of the N-terminal domain of Synechococcus elongatus SasA (average minimized structure)'''<br />
 
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==Overview==
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==Solution structure of the N-terminal domain of Synechococcus elongatus SasA (average minimized structure)==
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Circadian oscillators are endogenous biological systems that generate the approximately 24 hour temporal pattern of biological processes and confer a reproductive fitness advantage to their hosts. The cyanobacterial clock is the simplest known and the only clock system for which structural information for core component proteins, in this case KaiA, KaiB and KaiC, is available. SasA, a clock-associated histidine kinase, is necessary for robustness of the circadian rhythm of gene expression and implicated in clock output. The N-terminal domain of SasA (N-SasA) interacts directly with KaiC and likely functions as the sensory domain controlling the SasA histidine kinase activity. N-SasA and KaiB share significant sequence similarity and, thus, it has been proposed that they would be structurally similar and may even compete for KaiC binding. Here, we report the NMR structure of N-SasA and show it to be different from that of KaiB. The structural comparisons provide no clear details to suggest competition of SasA and KaiB for KaiC binding. N-SasA adopts a canonical thioredoxin fold but lacks the catalytic cysteine residues. A patch of conserved, solvent-exposed residues is found near the canonical thioredoxin active site. We suggest that this surface is used by N-SasA for protein-protein interactions. Our analysis suggests that the structural differences between N-SasA and KaiB are the result of only a few critical amino acid substitutions.
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<StructureSection load='1t4y' size='340' side='right'caption='[[1t4y]]' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1t4y]] 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=1T4Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T4Y FirstGlance]. <br>
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1T4Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of 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=1T4Y OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1t4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t4y OCA], [https://pdbe.org/1t4y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t4y RCSB], [https://www.ebi.ac.uk/pdbsum/1t4y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t4y ProSAT]</span></td></tr>
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==Reference==
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</table>
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Structure of the N-terminal domain of the circadian clock-associated histidine kinase SasA., Vakonakis I, Klewer DA, Williams SB, Golden SS, LiWang AC, J Mol Biol. 2004 Sep 3;342(1):9-17. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15313603 15313603]
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== Function ==
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[[Category: Single protein]]
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[https://www.uniprot.org/uniprot/SASA_SYNE7 SASA_SYNE7] May be involved in signal transduction. Participates in the KaiABC clock protein complex, which constitutes the main circadian regulator in cyanobacteria, via its interaction with KaiC. Required for robustness of the circadian rhythm of gene expression and is involved in clock outputs.<ref>PMID:10786837</ref>
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[[Category: Synechococcus elongatus]]
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== Evolutionary Conservation ==
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[[Category: Klewer, D A.]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: LiWang, A C.]]
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Check<jmol>
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[[Category: Vakonakis, I.]]
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<jmolCheckbox>
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[[Category: alpha/beta protein]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/t4/1t4y_consurf.spt"</scriptWhenChecked>
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[[Category: thioredoxin fold]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:09:56 2008''
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</jmolCheckbox>
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</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=1t4y ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Synechococcus elongatus PCC 7942 = FACHB-805]]
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[[Category: Klewer DA]]
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[[Category: LiWang AC]]
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[[Category: Vakonakis I]]

Current revision

Solution structure of the N-terminal domain of Synechococcus elongatus SasA (average minimized structure)

PDB ID 1t4y

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