View source for 2jqt


==Structure of the bacterial replication origin-associated protein Cnu==
<StructureSection load='2jqt' size='340' side='right'caption='[[2jqt]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2jqt]] 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=2JQT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JQT 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=2jqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jqt OCA], [https://pdbe.org/2jqt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jqt RCSB], [https://www.ebi.ac.uk/pdbsum/2jqt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jqt ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CNU_ECOLI CNU_ECOLI] The complex formed with H-NS binds to the specific 26-bp cnb site in the origin of replication oriC. Can complement, at least partially, the absence of the Hha protein in hha mutants.<ref>PMID:16199570</ref> 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jq/2jqt_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2jqt ConSurf].
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== Publication Abstract from PubMed ==
Cnu is a nucleoid protein that has a high degree of sequence homology with Hha/YmoA family proteins, which bind to chromatin and regulate the expression of Escherichia coli virulence genes in response to changes in temperature or ionic strength. Here, we determined its solution structure and dynamic properties and mapped H-NS binding sites. Cnu consists of three alpha helices that are comparable with those of Hha, but it has significant flexibility in the C-terminal region and lacks a short alpha helix present in Hha. Upon increasing ionic strength, the helical structure of Cnu is destabilized, especially at the ends of the helices. The dominant H-NS binding sites, located at helix 3 as in Hha, reveal a common structural platform for H-NS binding. Our results may provide structural and dynamic bases for the similarity and dissimilarity between Cnu and Hha functions.

Structure of the nucleoid-associated protein Cnu reveals common binding sites for H-NS in Cnu and Hha.,Bae SH, Liu D, Lim HM, Lee Y, Choi BS Biochemistry. 2008 Feb 19;47(7):1993-2001. Epub 2008 Jan 12. PMID:18189420<ref>PMID:18189420</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2jqt" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Bae SH]]
[[Category: Choi BS]]
[[Category: Lee Y]]
[[Category: Lim HM]]
[[Category: Liu D]]