1hns: Difference between revisions

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[[Image:1hns.gif|left|200px]]
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[[Image:1hns.png|left|200px]]


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{{STRUCTURE_1hns|  PDB=1hns  |  SCENE=  }}  
{{STRUCTURE_1hns|  PDB=1hns  |  SCENE=  }}  


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




==Overview==
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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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{{ABSTRACT_PUBMED_7875316}}


==About this Structure==
==About this Structure==
1HNS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HNS OCA].  
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==
==Reference==
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[[Category: Ueguchi, C.]]
[[Category: Ueguchi, C.]]
[[Category: Histone-like protein h1]]
[[Category: Histone-like protein h1]]
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Revision as of 08:26, 1 July 2008

File:1hns.png

Template:STRUCTURE 1hns

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

Template:ABSTRACT PUBMED 7875316

About this StructureAbout this Structure

1HNS is a Single protein structure of sequence from Escherichia coli. Full experimental information is available from OCA.

ReferenceReference

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

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