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6o8q

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Current revision (14:51, 13 March 2024) (edit) (undo)
 
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<StructureSection load='6o8q' size='340' side='right'caption='[[6o8q]], [[Resolution|resolution]] 3.22&Aring;' scene=''>
<StructureSection load='6o8q' size='340' side='right'caption='[[6o8q]], [[Resolution|resolution]] 3.22&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6o8q]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O8Q OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6O8Q FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6o8q]] is a 12 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=6O8Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6O8Q FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hupA, b4000, JW3964 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.216&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6o8q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o8q OCA], [http://pdbe.org/6o8q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6o8q RCSB], [http://www.ebi.ac.uk/pdbsum/6o8q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6o8q ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6o8q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o8q OCA], [https://pdbe.org/6o8q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6o8q RCSB], [https://www.ebi.ac.uk/pdbsum/6o8q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6o8q ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://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.
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[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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6o8q" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ecoli]]
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[[Category: Escherichia coli]]
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[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Hammel, M]]
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[[Category: Hammel M]]
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[[Category: Remesh, S G]]
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[[Category: Remesh SG]]
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[[Category: Dna binding protein]]
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[[Category: Dna binding protein-dna complex]]
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[[Category: Dna supercoiling]]
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[[Category: Histone like protein]]
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[[Category: Nucleoid associated protein]]
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Current revision

HUaa 19bp SYM DNA pH 4.5

PDB ID 6o8q

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