View source for 6oaj


==HUaE34K 19bp SYM DNA==
<StructureSection load='6oaj' size='340' side='right'caption='[[6oaj]], [[Resolution|resolution]] 4.09&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6oaj]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OAJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OAJ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.092&#8491;</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=6oaj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oaj OCA], [https://pdbe.org/6oaj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6oaj RCSB], [https://www.ebi.ac.uk/pdbsum/6oaj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6oaj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DBHA_ECOLI DBHA_ECOLI] Histone-like DNA-binding protein which is capable of wrapping DNA to stabilize it, and thus to prevent its denaturation under extreme environmental conditions.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacterial nucleoid remodeling dependent on conserved histone-like protein, HU is one of the determining factors in global gene regulation. By imaging of near-native, unlabeled E. coli cells by soft X-ray tomography, we show that HU remodels nucleoids by promoting the formation of a dense condensed core surrounded by less condensed isolated domains. Nucleoid remodeling during cell growth and environmental adaptation correlate with pH and ionic strength controlled molecular switch that regulated HUalphaalpha dependent intermolecular DNA bundling. Through crystallographic and solution-based studies we show that these effects mechanistically rely on HUalphaalpha promiscuity in forming multiple electrostatically driven multimerization interfaces. Changes in DNA bundling consequently affects gene expression globally, likely by constrained DNA supercoiling. Taken together our findings unveil a critical function of HU-DNA interaction in nucleoid remodeling that may serve as a general microbial mechanism for transcriptional regulation to synchronize genetic responses during the cell cycle and adapt to changing environments.

Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling.,Remesh SG, Verma SC, Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M Nat Commun. 2020 Jun 9;11(1):2905. doi: 10.1038/s41467-020-16724-5. PMID:32518228<ref>PMID:32518228</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6oaj" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Hammel M]]
[[Category: Remesh SG]]