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==Backbone structure of the membrane domain of E. coli histidine kinase receptor QseC, Center for Structures of Membrane Proteins (CSMP) target 4311C==
==Backbone structure of the membrane domain of E. coli histidine kinase receptor QseC, Center for Structures of Membrane Proteins (CSMP) target 4311C==
<StructureSection load='2kse' size='340' side='right' caption='[[2kse]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='2kse' size='340' side='right'caption='[[2kse]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2kse]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KSE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KSE FirstGlance]. <br>
<table><tr><td colspan='2'>[[2kse]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KSE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KSE FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b3026, JW2994, qseC, ygiY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidine_kinase Histidine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.13.3 2.7.13.3] </span></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=2kse FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kse OCA], [https://pdbe.org/2kse PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kse RCSB], [https://www.ebi.ac.uk/pdbsum/2kse PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kse ProSAT]</span></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=2kse FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kse OCA], [http://pdbe.org/2kse PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2kse RCSB], [http://www.ebi.ac.uk/pdbsum/2kse PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/QSEC_ECOLI QSEC_ECOLI]] Member of a two-component regulatory system QseB/QseC. Activates the flagella regulon by activating transcription of FlhDC. May activate QseB by phosphorylation.<ref>PMID:11929534</ref>
[https://www.uniprot.org/uniprot/QSEC_ECOLI QSEC_ECOLI] Member of a two-component regulatory system QseB/QseC. Activates the flagella regulon by activating transcription of FlhDC. May activate QseB by phosphorylation.<ref>PMID:11929534</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ks/2kse_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ks/2kse_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
Line 19: Line 19:
</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=2kse ConSurf].
</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=2kse ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
NMR structural studies of membrane proteins (MP) are hampered by complications in MP expression, technical difficulties associated with the slow process of NMR spectral peak assignment, and limited distance information obtainable for transmembrane (TM) helices. To overcome the inherent challenges in the determination of MP structures, we have developed a rapid and cost-efficient strategy that combines cell-free (CF) protein synthesis, optimized combinatorial dual-isotope labeling for nearly instant resonance assignment, and fast acquisition of long-distance information using paramagnetic probes. Here we report three backbone structures for the TM domains of the three classes of Escherichia coli histidine kinase receptors (HKRs). The ArcB and QseC TM domains are both two-helical motifs, whereas the KdpD TM domain comprises a four-helical bundle with shorter second and third helices. The interhelical distances (up to 12 A) reveal weak interactions within the TM domains of all three receptors. Determined consecutively within 8 months, these structures offer insight into the abundant and underrepresented in the Protein Data Bank class of 2-4 TM crossers and demonstrate the efficiency of our CF combinatorial dual-labeling strategy, which can be applied to solve MP structures in high numbers and at a high speed. Our results greatly expand the current knowledge of HKR structure, opening the doors to studies on their widespread and pharmaceutically important bacterial signaling mechanism.
Membrane domain structures of three classes of histidine kinase receptors by cell-free expression and rapid NMR analysis.,Maslennikov I, Klammt C, Hwang E, Kefala G, Okamura M, Esquivies L, Mors K, Glaubitz C, Kwiatkowski W, Jeon YH, Choe S Proc Natl Acad Sci U S A. 2010 Jun 15;107(24):10902-7. Epub 2010 May 24. PMID:20498088<ref>PMID:20498088</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2kse" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Ecoli]]
[[Category: Escherichia coli K-12]]
[[Category: Histidine kinase]]
[[Category: Large Structures]]
[[Category: CSMP, Center for Structures of Membrane Proteins]]
[[Category: Choe S]]
[[Category: Choe, S]]
[[Category: Esquivies L]]
[[Category: Esquivies, L]]
[[Category: Kefala G]]
[[Category: Kefala, G]]
[[Category: Klammt C]]
[[Category: Klammt, C]]
[[Category: Kwiatkowski W]]
[[Category: Kwiatkowski, W]]
[[Category: Maslennikov I]]
[[Category: Maslennikov, I]]
[[Category: Atp-binding]]
[[Category: Cell inner membrane]]
[[Category: Cell membrane]]
[[Category: Cell-free synthesis]]
[[Category: Center for structures of membrane protein]]
[[Category: Csmp]]
[[Category: Histidine kinase receptor]]
[[Category: Kinase]]
[[Category: Membrane]]
[[Category: Membrane domain]]
[[Category: Methods development]]
[[Category: Nucleotide-binding]]
[[Category: Phosphoprotein]]
[[Category: PSI, Protein structure initiative]]
[[Category: Structural genomic]]
[[Category: Transferase]]
[[Category: Transmembrane]]
[[Category: Two-component regulatory system]]
[[Category: Two-helical hairpin]]
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