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| ==Chemical Shift and Structure Assignments for Sma0114== | | ==Chemical Shift and Structure Assignments for Sma0114== |
| <StructureSection load='2lpm' size='340' side='right' caption='[[2lpm]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | | <StructureSection load='2lpm' size='340' side='right'caption='[[2lpm]]' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[2lpm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sinorhizobium_meliloti Sinorhizobium meliloti]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LPM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LPM FirstGlance]. <br> | | <table><tr><td colspan='2'>[[2lpm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sinorhizobium_meliloti_1021 Sinorhizobium meliloti 1021]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LPM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LPM FirstGlance]. <br> |
| </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RA0058, SMa0114 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=382 Sinorhizobium meliloti])</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='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=2lpm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lpm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lpm RCSB], [http://www.ebi.ac.uk/pdbsum/2lpm PDBsum]</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=2lpm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lpm OCA], [https://pdbe.org/2lpm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lpm RCSB], [https://www.ebi.ac.uk/pdbsum/2lpm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lpm ProSAT]</span></td></tr> |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| | == Function == |
| == Publication Abstract from PubMed == | | [https://www.uniprot.org/uniprot/Q930Y6_RHIME Q930Y6_RHIME] |
| Receiver domains control intracellular responses triggered by signal transduction in bacterial two-component systems. Here, we report the solution nuclear magnetic resonance structure and dynamics of Sma0114 from the bacterium Sinorhizobium meliloti, the first such characterization of a receiver domain from the HWE-kinase family of two-component systems. The structure of Sma0114 adopts a prototypical alpha(5)/beta(5) Rossman fold but has features that set it apart from other receiver domains. The fourth beta-strand of Sma0114 houses a PFxFATGY sequence motif, common to many HWE-kinase-associated receiver domains. This sequence motif in Sma0114 may substitute for the conserved Y-T coupling mechanism, which propagates conformational transitions in the 455 (alpha4-beta5-alpha5) faces of receiver domains, to prime them for binding downstream effectors once they become activated by phosphorylation. In addition, the fourth alpha-helix of the consensus 455 face in Sma0114 is replaced with a segment that shows high flexibility on the pico- to nanosecond time scale by (15)N relaxation data. Secondary structure prediction analysis suggests that the absence of helix alpha4 may be a conserved property of the HWE-kinase-associated family of receiver domains to which Sma0114 belongs. In spite of these differences, Sma0114 has a conserved active site, binds divalent metal ions such as Mg(2+) and Ca(2+) that are required for phosphorylation, and exhibits micro- to millisecond active-site dynamics similar to those of other receiver domains. Taken together, our results suggest that Sma0114 has a conserved active site but differs from typical receiver domains in the structure of the 455 face that is used to effect signal transduction following activation.
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| Nuclear Magnetic Resonance Structure and Dynamics of the Response Regulator Sma0114 from Sinorhizobium meliloti.,Sheftic SR, Garcia PP, White E, Robinson VL, Gage DJ, Alexandrescu AT Biochemistry. 2012 Sep 4;51(35):6932-41. Epub 2012 Aug 21. PMID:22880754<ref>PMID:22880754</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| ==See Also== | | ==See Also== |
| *[[Response regulator|Response regulator]] | | *[[Response regulator 3D structure|Response regulator 3D structure]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Sinorhizobium meliloti]] | | [[Category: Large Structures]] |
| [[Category: Alexandrescu, A T]] | | [[Category: Sinorhizobium meliloti 1021]] |
| [[Category: Gage, D J]] | | [[Category: Alexandrescu AT]] |
| [[Category: Sheftic, S R]] | | [[Category: Gage DJ]] |
| [[Category: Transcription regulator]] | | [[Category: Sheftic SR]] |