1pux: Difference between revisions
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New page: left|200px<br /><applet load="1pux" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pux" /> '''NMR Solution Structure of BeF3-Activated Spo... |
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== | ==NMR Solution Structure of BeF3-Activated Spo0F, 20 conformers== | ||
Two-component systems, which are comprised of a single histidine-aspartate | <StructureSection load='1pux' size='340' side='right'caption='[[1pux]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1pux]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PUX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PUX 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=1pux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pux OCA], [https://pdbe.org/1pux PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pux RCSB], [https://www.ebi.ac.uk/pdbsum/1pux PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pux ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SP0F_BACSU SP0F_BACSU] Key element in the phosphorelay regulating sporulation initiation. Phosphorylation of spo0B during sporulation initiation. | |||
== 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/pu/1pux_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=1pux ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Two-component systems, which are comprised of a single histidine-aspartate phosphotransfer module, are the dominant signaling pathways in bacteria and have recently been identified in several eukaryotic organisms as well. A tandem connection of two or more histidine-aspartate motifs forms complex phosphorelays. While response regulators from simple two-component systems have been characterized structurally in their inactive and active forms, we address here the question of whether a response regulator from a phosphorelay has a distinct structural basis of activation. We report the NMR solution structure of BeF(3)(-)-activated Spo0F, the first structure of a response regulator from a phosphorelay in its activated state. Conformational changes were found in regions previously identified to change in simple two-component systems. In addition, a downward shift by half a helical turn in helix 1, located on the opposite side of the common activation surface, was observed as a consequence of BeF(3)(-) activation. Conformational changes in helix 1 can be rationalized by the distinct function of phosphoryl transfer to the second histidine kinase, Spo0B, because helix 1 is known to interact directly with Spo0B and the phosphatase RapB. The identification of structural rearrangements in Spo0F supports the hypothesis of a pre-existing equilibrium between the inactive and active state prior to phosphorylation that was suggested on the basis of previous NMR dynamics studies on Spo0F. A shift of a pre-existing equilibrium is likely a general feature of response regulators. | |||
The NMR solution structure of BeF(3)(-)-activated Spo0F reveals the conformational switch in a phosphorelay system.,Gardino AK, Volkman BF, Cho HS, Lee SY, Wemmer DE, Kern D J Mol Biol. 2003 Aug 1;331(1):245-54. PMID:12875849<ref>PMID:12875849</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1pux" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Phosphotransferase 3D structures|Phosphotransferase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Cho | [[Category: Cho HS]] | ||
[[Category: Gardino | [[Category: Gardino AK]] | ||
[[Category: Kern | [[Category: Kern D]] | ||
[[Category: Lee | [[Category: Lee SY]] | ||
[[Category: Volkman | [[Category: Volkman BF]] | ||
[[Category: Wemmer | [[Category: Wemmer DE]] | ||
