1hns: Difference between revisions

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{{Seed}}
[[Image:1hns.png|left|200px]]


<!--
==H-NS (DNA-BINDING DOMAIN)==
The line below this paragraph, containing "STRUCTURE_1hns", creates the "Structure Box" on the page.
<StructureSection load='1hns' size='340' side='right'caption='[[1hns]]' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1hns]] 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=1HNS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HNS FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1hns FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hns OCA], [https://pdbe.org/1hns PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hns RCSB], [https://www.ebi.ac.uk/pdbsum/1hns PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hns ProSAT]</span></td></tr>
{{STRUCTURE_1hns|  PDB=1hns  |  SCENE=  }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/HNS_ECOLI HNS_ECOLI] A DNA-binding protein implicated in transcriptional repression (silencing) as well as in bacterial chromosome organization. H-NS binds tightly to AT-rich dsDNA, increases its thermal stability and inhibits transcription. Also binds to ssDNA 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. Plays a role in the thermal control of pili and adhesive curli fimbriae production, by inducing transcription of csgD. Represses the CRISPR-cas promoters, permits only weak transcription of the crRNA precursor; its role is antagonized by LeuO. Subject to transcriptional auto-repression. Binds preferentially to the upstream region of its own gene recognizing two segments of DNA on both sides of a bend centered around -150.<ref>PMID:7934818</ref> <ref>PMID:11031114</ref> <ref>PMID:17010156</ref> <ref>PMID:20659289</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/hn/1hns_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=1hns ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The three-dimensional structure of the C-terminal domain (47 residues) obtained from the hydrolysis of H-NS protein with bovine trypsin was determined by NMR measurements and distance geometry calculations. It is composed of an antiparallel beta-sheet, an alpha-helix and a 3(10)-helix which form a hydrophobic core, stabilizing the whole structure. This domain has been found to bind to DNA. Possible DNA binding sites are discussed on the basis of the solution structure of the C-terminal domain of H-NS.


===H-NS (DNA-BINDING DOMAIN)===
Solution structure of the DNA binding domain of a nucleoid-associated protein, H-NS, from Escherichia coli.,Shindo H, Iwaki T, Ieda R, Kurumizaka H, Ueguchi C, Mizuno T, Morikawa S, Nakamura H, Kuboniwa H FEBS Lett. 1995 Feb 27;360(2):125-31. PMID:7875316<ref>PMID:7875316</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
<!--
</div>
The line below this paragraph, {{ABSTRACT_PUBMED_7875316}}, adds the Publication Abstract to the page
<div class="pdbe-citations 1hns" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 7875316 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_7875316}}
__TOC__
 
</StructureSection>
==About this Structure==
1HNS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HNS OCA].
 
==Reference==
Solution structure of the DNA binding domain of a nucleoid-associated protein, H-NS, from Escherichia coli., Shindo H, Iwaki T, Ieda R, Kurumizaka H, Ueguchi C, Mizuno T, Morikawa S, Nakamura H, Kuboniwa H, FEBS Lett. 1995 Feb 27;360(2):125-31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7875316 7875316]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Ieda, R.]]
[[Category: Ieda R]]
[[Category: Iwaki, T.]]
[[Category: Iwaki T]]
[[Category: Kuboniwa, H.]]
[[Category: Kuboniwa H]]
[[Category: Kurumizaka, H.]]
[[Category: Kurumizaka H]]
[[Category: Mizuno, T.]]
[[Category: Mizuno T]]
[[Category: Morikawa, S.]]
[[Category: Morikawa S]]
[[Category: Nakamura, H.]]
[[Category: Nakamura H]]
[[Category: Shindo, H.]]
[[Category: Shindo H]]
[[Category: Ueguchi, C.]]
[[Category: Ueguchi C]]
[[Category: Histone-like protein h1]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 08:26:45 2008''

Latest revision as of 11:32, 22 May 2024

H-NS (DNA-BINDING DOMAIN)H-NS (DNA-BINDING DOMAIN)

Structural highlights

1hns is a 1 chain structure with sequence from Escherichia coli. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HNS_ECOLI A DNA-binding protein implicated in transcriptional repression (silencing) as well as in bacterial chromosome organization. H-NS binds tightly to AT-rich dsDNA, increases its thermal stability and inhibits transcription. Also binds to ssDNA 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. Plays a role in the thermal control of pili and adhesive curli fimbriae production, by inducing transcription of csgD. Represses the CRISPR-cas promoters, permits only weak transcription of the crRNA precursor; its role is antagonized by LeuO. Subject to transcriptional auto-repression. Binds preferentially to the upstream region of its own gene recognizing two segments of DNA on both sides of a bend centered around -150.[1] [2] [3] [4]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The three-dimensional structure of the C-terminal domain (47 residues) obtained from the hydrolysis of H-NS protein with bovine trypsin was determined by NMR measurements and distance geometry calculations. It is composed of an antiparallel beta-sheet, an alpha-helix and a 3(10)-helix which form a hydrophobic core, stabilizing the whole structure. This domain has been found to bind to DNA. Possible DNA binding sites are discussed on the basis of the solution structure of the C-terminal domain of H-NS.

Solution structure of the DNA binding domain of a nucleoid-associated protein, H-NS, from Escherichia coli.,Shindo H, Iwaki T, Ieda R, Kurumizaka H, Ueguchi C, Mizuno T, Morikawa S, Nakamura H, Kuboniwa H FEBS Lett. 1995 Feb 27;360(2):125-31. PMID:7875316[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Falconi M, Higgins NP, Spurio R, Pon CL, Gualerzi CO. Expression of the gene encoding the major bacterial nucleotide protein H-NS is subject to transcriptional auto-repression. Mol Microbiol. 1993 Oct;10(2):273-82. PMID:7934818
  2. ↑ Ko M, Park C. Two novel flagellar components and H-NS are involved in the motor function of Escherichia coli. J Mol Biol. 2000 Oct 27;303(3):371-82. PMID:11031114 doi:http://dx.doi.org/10.1006/jmbi.2000.4147
  3. ↑ Weber H, Pesavento C, Possling A, Tischendorf G, Hengge R. Cyclic-di-GMP-mediated signalling within the sigma network of Escherichia coli. Mol Microbiol. 2006 Nov;62(4):1014-34. Epub 2006 Sep 29. PMID:17010156 doi:http://dx.doi.org/MMI5440
  4. ↑ Westra ER, Pul U, Heidrich N, Jore MM, Lundgren M, Stratmann T, Wurm R, Raine A, Mescher M, Van Heereveld L, Mastop M, Wagner EG, Schnetz K, Van Der Oost J, Wagner R, Brouns SJ. H-NS-mediated repression of CRISPR-based immunity in Escherichia coli K12 can be relieved by the transcription activator LeuO. Mol Microbiol. 2010 Sep;77(6):1380-93. doi: 10.1111/j.1365-2958.2010.07315.x., Epub 2010 Aug 18. PMID:20659289 doi:http://dx.doi.org/10.1111/j.1365-2958.2010.07315.x
  5. ↑ Shindo H, Iwaki T, Ieda R, Kurumizaka H, Ueguchi C, Mizuno T, Morikawa S, Nakamura H, Kuboniwa H. Solution structure of the DNA binding domain of a nucleoid-associated protein, H-NS, from Escherichia coli. FEBS Lett. 1995 Feb 27;360(2):125-31. PMID:7875316
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