3nr7

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{{STRUCTURE_3nr7| PDB=3nr7 | SCENE= }}
 
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===Crystal structure of S. typhimurium H-NS 1-83===
 
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{{ABSTRACT_PUBMED_20798056}}
 
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==About this Structure==
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==Crystal structure of S. typhimurium H-NS 1-83==
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[[3nr7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_typhimurium Salmonella enterica subsp. enterica serovar typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NR7 OCA].
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<StructureSection load='3nr7' size='340' side='right'caption='[[3nr7]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3nr7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NR7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NR7 FirstGlance]. <br>
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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]] 3.7&#8491;</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=3nr7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nr7 OCA], [https://pdbe.org/3nr7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nr7 RCSB], [https://www.ebi.ac.uk/pdbsum/3nr7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nr7 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HNS_SALTY HNS_SALTY] H-NS binds tightly to ds-DNA, increases its thermal stability and inhibits transcription. It also binds to ss-DNA and RNA but with a much lower affinity. H-NS has possible histone-like function. May be a global transcriptional regulator through its ability to bind to curved DNA sequences, which are found in regions upstream of a certain subset of promoters. It plays a role in the thermal control of pili production. It is subject to transcriptional auto-repression. It binds preferentially to the upstream region of its own gene recognizing two segments of DNA on both sides of a bend centered around -150 (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nr/3nr7_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=3nr7 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The histone-like nucleoid structuring (H-NS) protein plays a fundamental role in DNA condensation and is a key regulator of enterobacterial gene expression in response to changes in osmolarity, pH, and temperature. The protein is capable of high-order self-association via interactions of its oligomerization domain. Using crystallography, we have solved the structure of this complete domain in an oligomerized state. The observed superhelical structure establishes a mechanism for the self-association of H-NS via both an N-terminal antiparallel coiled-coil and a second, hitherto unidentified, helix-turn-helix dimerization interface at the C-terminal end of the oligomerization domain. The helical scaffold suggests the formation of a H-NS:plectonemic DNA nucleoprotein complex that is capable of explaining published biophysical and functional data, and establishes a unifying structural basis for coordinating the DNA packaging and transcription repression functions of H-NS.
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==Reference==
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H-NS forms a superhelical protein scaffold for DNA condensation.,Arold ST, Leonard PG, Parkinson GN, Ladbury JE Proc Natl Acad Sci U S A. 2010 Sep 7;107(36):15728-32. Epub 2010 Aug 23. PMID:20798056<ref>PMID:20798056</ref>
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<ref group="xtra">PMID:020798056</ref><references group="xtra"/><references/>
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[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Arold, S T.]]
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</div>
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[[Category: Ladbury, J E.]]
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<div class="pdbe-citations 3nr7" style="background-color:#fffaf0;"></div>
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[[Category: Leonard, P G.]]
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== References ==
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[[Category: Parkinson, G N.]]
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<references/>
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[[Category: Dimer]]
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__TOC__
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[[Category: Dna binding protein]]
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</StructureSection>
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[[Category: Dna condensation]]
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[[Category: Large Structures]]
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[[Category: Oligomerisation]]
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[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
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[[Category: Arold ST]]
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[[Category: Ladbury JE]]
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[[Category: Leonard PG]]
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[[Category: Parkinson GN]]

Current revision

Crystal structure of S. typhimurium H-NS 1-83

PDB ID 3nr7

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