1hns
From Proteopedia
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| - | [[Image:1hns.png|left|200px]] | ||
| - | + | ==H-NS (DNA-BINDING DOMAIN)== | |
| + | <StructureSection load='1hns' size='340' side='right'caption='[[1hns]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <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> | ||
| + | </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=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> | ||
| + | </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. | ||
| - | + | 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1hns" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | == | + | __TOC__ |
| - | < | + | </StructureSection> |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| - | [[Category: Ieda | + | [[Category: Large Structures]] |
| - | [[Category: Iwaki | + | [[Category: Ieda R]] |
| - | [[Category: Kuboniwa | + | [[Category: Iwaki T]] |
| - | [[Category: Kurumizaka | + | [[Category: Kuboniwa H]] |
| - | [[Category: Mizuno | + | [[Category: Kurumizaka H]] |
| - | [[Category: Morikawa | + | [[Category: Mizuno T]] |
| - | [[Category: Nakamura | + | [[Category: Morikawa S]] |
| - | [[Category: Shindo | + | [[Category: Nakamura H]] |
| - | [[Category: Ueguchi | + | [[Category: Shindo H]] |
| - | + | [[Category: Ueguchi C]] | |
| - | + | ||
Current revision
H-NS (DNA-BINDING DOMAIN)
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Categories: Escherichia coli | Large Structures | Ieda R | Iwaki T | Kuboniwa H | Kurumizaka H | Mizuno T | Morikawa S | Nakamura H | Shindo H | Ueguchi C
