2m98: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2m98]] 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=2M98 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M98 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2m98]] 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=2M98 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M98 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=2m98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m98 OCA], [https://pdbe.org/2m98 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m98 RCSB], [https://www.ebi.ac.uk/pdbsum/2m98 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m98 ProSAT]</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=2m98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m98 OCA], [https://pdbe.org/2m98 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m98 RCSB], [https://www.ebi.ac.uk/pdbsum/2m98 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m98 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/Q930Y6_RHIME Q930Y6_RHIME]  
[https://www.uniprot.org/uniprot/Q930Y6_RHIME Q930Y6_RHIME]  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacterial receiver domains modulate intracellular responses to external stimuli in two-component systems. Sma0114 is the first structurally characterized representative from the family of receiver domains that are substrates for histidine-tryptophan-glutamate (HWE) kinases. We report the NMR structure of Sma0114 bound by Ca(2+) and BeF3(-), a phosphate analogue that stabilizes the activated state. Differences between the NMR structures of the inactive and activated states occur in helix alpha1, the active site loop that connects strand beta3 and helix alpha3, and in the segment from strand beta5 to helix alpha5 of the 455 (alpha4-beta5-alpha5) face. Structural rearrangements of the 455 face typically make receiver domains competent for binding downstream target molecules. In Sma0114 the structural changes accompanying activation result in a more negatively charged surface for the 455 face. Coupling between the 455 face and active site phosphorylation is usually mediated through the rearrangement of a threonine and tyrosine residue, in a mechanism called Y-T coupling. The NMR structure indicates that Sma0114 lacks Y-T coupling and that communication between the active site and the 455 face is achieved through a conserved lysine residue that stabilizes the acyl phosphate in receiver domains. (15)N-NMR relaxation experiments were used to investigate the backbone dynamics of the Sma0114 apoprotein, the binary Sma0114.Ca(2+) complex, and the ternary Sma0114.Ca(2+).BeF3(-) complex. The loss of entropy due to ligand binding at the active site is compensated by increased flexibility in the 455 face. The dynamic character of the 455 face in Sma0114, which results in part from the replacement of helix alpha4 by a flexible loop, may facilitate induced-fit recognition of target molecules.
NMR Structure of the HWE Kinase Associated Response Regulator Sma0114 in Its Activated State.,Sheftic SR, White E, Gage DJ, Alexandrescu AT Biochemistry. 2014 Jan 21;53(2):311-22. doi: 10.1021/bi401497h. Epub 2014 Jan 6. PMID:24364624<ref>PMID:24364624</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2m98" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Response regulator 3D structure|Response regulator 3D structure]]
*[[Response regulator 3D structure|Response regulator 3D structure]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Revision as of 06:59, 1 May 2024

NMR Structure of BeF3 Activated Sma0114

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