1hns: Difference between revisions
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<StructureSection load='1hns' size='340' side='right'caption='[[1hns]], [[NMR_Ensembles_of_Models | 16 NMR models]]' scene=''> | <StructureSection load='1hns' size='340' side='right'caption='[[1hns]], [[NMR_Ensembles_of_Models | 16 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1hns]] is a 1 chain structure. 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> | <table><tr><td colspan='2'>[[1hns]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. 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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1hnr|1hnr]]</div></td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1hnr|1hnr]]</div></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> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bacillus coli migula 1895]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Ieda, R]] | [[Category: Ieda, R]] | ||
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[[Category: Shindo, H]] | [[Category: Shindo, H]] | ||
[[Category: Ueguchi, C]] | [[Category: Ueguchi, C]] | ||
[[Category: Dna binding protein]] | |||
[[Category: Dna-binding protein]] | [[Category: Dna-binding protein]] | ||
[[Category: Histone-like protein h1]] | [[Category: Histone-like protein h1]] | ||
Revision as of 10:53, 23 February 2022
H-NS (DNA-BINDING DOMAIN)H-NS (DNA-BINDING DOMAIN)
Structural highlights
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 PubMedThe 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
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