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The | ==NMR Solution Structure of Cold Shock Protein CspA== | ||
<StructureSection load='30ib' size='340' side='right'caption='[[30ib]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[30ib]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=30IB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=30IB FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, models</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=30ib FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=30ib OCA], [https://pdbe.org/30ib PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=30ib RCSB], [https://www.ebi.ac.uk/pdbsum/30ib PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=30ib ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CSPA_ECOLI CSPA_ECOLI] Binds to and stimulates the transcription of the CCAAT-containing, cold-shock-inducible promoters of the H-NS and GyrA proteins. Binds also to the inverted repeat 5'-ATTGG-3'. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Cold-shock proteins (CSPs) are highly conserved nucleic acid-binding proteins that act as chaperones during cellular adaptation to low temperatures. Here, we present a comprehensive structural and dynamic characterization of Escherichia coli CspA using high-resolution NMR spectroscopy. The solution structure of CspA (PDB ID: 30IB) is supported by extensive NMR experimental restraints, minimal violations, and favorable stereochemistry, establishing it as a well-converged NMR structure. Crucially, we investigated backbone dynamics across multiple timescales, with a particular focus on the microsecond-millisecond regime using a combination of (15)N Carr-Purcell-Meiboom-Gill (CPMG) relaxation dispersion and (15)N chemical exchange saturation transfer (CEST) experiments, together with visible peak-position constraints. To our knowledge, this represents the first application of such a combined (15)N CEST, (15)N CPMG and visible peak-position constraints approach to probe conformational exchange in CSPs. Our results show that, in addition to the conserved aromatic residues of RNP1 and RNP2 motifs that mediate pi-stacking interactions with nucleic acids, an unexpectedly broad network of hydrophobic core and solvent-exposed polar residues undergoes conformational exchange. Notably, residues in the beta3-beta4 and beta4-beta5 loops display complex dynamics not fully captured by model-free analysis formalism, highlighting their role in binding site flexibility. Complementary AF3/YASARA modeling of the CspA bound to heptathymidine (dT7) further supported that aromatic and polar residues form pi-stacking and ionic interactions with ssDNA bases, corroborating the functional relevance of these dynamic regions. Therefore, our findings demonstrate that CspA relies on a dynamic network extending from conserved motifs through the hydrophobic core and flexible loops, conferring the structural adaptability required for efficient nucleic acid recognition and chaperone activity. | |||
Structural and functional insights into a mesophilic cold shock protein CspA with enhanced precision.,Wanko Nembot M, Feller G, Volkov AN, le Paige UB, Bouvignies G, Damblon C J Magn Reson. 2026 May 1;388:108077. doi: 10.1016/j.jmr.2026.108077. PMID:42102648<ref>PMID:42102648</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 30ib" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | |||
[[Category: Large Structures]] | |||
[[Category: Dambon C]] | |||
[[Category: Feller G]] | |||
[[Category: Volkov O]] | |||
[[Category: Wanko M]] | |||
