2ksf
From Proteopedia
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==Backbone structure of the membrane domain of E. coli histidine kinase receptor KdpD, Center for Structures of Membrane Proteins (CSMP) target 4312C== | ==Backbone structure of the membrane domain of E. coli histidine kinase receptor KdpD, Center for Structures of Membrane Proteins (CSMP) target 4312C== | ||
- | <StructureSection load='2ksf' size='340' side='right' caption='[[2ksf | + | <StructureSection load='2ksf' size='340' side='right'caption='[[2ksf]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[2ksf]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2ksf]] 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=2KSF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KSF FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </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=2ksf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ksf OCA], [https://pdbe.org/2ksf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ksf RCSB], [https://www.ebi.ac.uk/pdbsum/2ksf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ksf ProSAT]</span></td></tr> | |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
- | [ | + | [https://www.uniprot.org/uniprot/KDPD_ECOLI KDPD_ECOLI] Member of the two-component regulatory system KdpD/KdpE involved in the regulation of the kdp operon. KdpD may function as a membrane-associated protein kinase that phosphorylates KdpE in response to environmental signals. |
== 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/2ksf_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ks/2ksf_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> | ||
</jmolCheckbox> | </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/ | + | </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=2ksf 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. | ||
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- | 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> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: Escherichia coli | + | [[Category: Escherichia coli K-12]] |
- | [[Category: | + | [[Category: Large Structures]] |
- | + | [[Category: Choe S]] | |
- | [[Category: Choe | + | [[Category: Esquivies L]] |
- | [[Category: Esquivies | + | [[Category: Kefala G]] |
- | [[Category: Kefala | + | [[Category: Klammt C]] |
- | [[Category: Klammt | + | [[Category: Kwiatkowski W]] |
- | [[Category: Kwiatkowski | + | [[Category: Maslennikov I]] |
- | [[Category: Maslennikov | + | [[Category: Okamura M]] |
- | [[Category: Okamura | + | |
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Current revision
Backbone structure of the membrane domain of E. coli histidine kinase receptor KdpD, Center for Structures of Membrane Proteins (CSMP) target 4312C
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