View source for 2msk


==Solution Structure and Chemical Shift Assignments for BeF3 activated Receiver Domain of Nitrogen Regulatory Protein C (NtrC) at 35C==
<StructureSection load='2msk' size='340' side='right'caption='[[2msk]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2msk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._UK-1 Salmonella enterica subsp. enterica serovar Typhimurium str. UK-1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MSK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MSK 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=2msk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2msk OCA], [https://pdbe.org/2msk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2msk RCSB], [https://www.ebi.ac.uk/pdbsum/2msk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2msk ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0M3KKS6_SALTU A0A0M3KKS6_SALTU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The interconversion between inactive and active protein states, traditionally described by two static structures, is at the heart of signalling. However, how folded states interconvert is largely unknown due to the inability to experimentally observe transition pathways. Here we explore the free energy landscape of the bacterial response regulator NtrC by combining computation and nuclear magnetic resonance, and discover unexpected features underlying efficient signalling. We find that functional states are defined purely in kinetic and not structural terms. The need of a well-defined conformer, crucial to the active state, is absent in the inactive state, which comprises a heterogeneous collection of conformers. The transition between active and inactive states occurs through multiple pathways, facilitated by a number of nonnative transient hydrogen bonds, thus lowering the transition barrier through both entropic and enthalpic contributions. These findings may represent general features for functional conformational transitions within the folded state.

Free energy landscape of activation in a signalling protein at atomic resolution.,Pontiggia F, Pachov DV, Clarkson MW, Villali J, Hagan MF, Pande VS, Kern D Nat Commun. 2015 Jun 15;6:7284. doi: 10.1038/ncomms8284. PMID:26073309<ref>PMID:26073309</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2msk" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. UK-1]]
[[Category: Clarkson MW]]
[[Category: Kern D]]
[[Category: Pontiggia F]]
[[Category: Villali J]]