1hns
From Proteopedia
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==H-NS (DNA-BINDING DOMAIN)== | ==H-NS (DNA-BINDING DOMAIN)== | ||
| - | <StructureSection load='1hns' size='340' side='right'caption='[[1hns | + | <StructureSection load='1hns' size='340' side='right'caption='[[1hns]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1hns]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <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=' | + | </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> | <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> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=1hns ConSurf]. | </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="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. | ||
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| - | 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> | ||
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| - | 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 == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Escherichia coli]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Ieda | + | [[Category: Ieda R]] |
| - | [[Category: Iwaki | + | [[Category: Iwaki T]] |
| - | [[Category: Kuboniwa | + | [[Category: Kuboniwa H]] |
| - | [[Category: Kurumizaka | + | [[Category: Kurumizaka H]] |
| - | [[Category: Mizuno | + | [[Category: Mizuno T]] |
| - | [[Category: Morikawa | + | [[Category: Morikawa S]] |
| - | [[Category: Nakamura | + | [[Category: Nakamura H]] |
| - | [[Category: Shindo | + | [[Category: Shindo H]] |
| - | [[Category: Ueguchi | + | [[Category: Ueguchi C]] |
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Revision as of 11:33, 27 March 2024
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
