1hns: Difference between revisions
New page: left|200px<br /><applet load="1hns" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hns" /> '''H-NS (DNA-BINDING DOMAIN)'''<br /> ==Overvi... |
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[[Image:1hns.gif|left|200px]]<br /><applet load="1hns" size=" | [[Image:1hns.gif|left|200px]]<br /><applet load="1hns" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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'''H-NS (DNA-BINDING DOMAIN)'''<br /> | '''H-NS (DNA-BINDING DOMAIN)'''<br /> | ||
==Overview== | ==Overview== | ||
The three-dimensional structure of the C-terminal domain (47 residues) | 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. | ||
==About this Structure== | ==About this Structure== | ||
1HNS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | 1HNS is a [http://en.wikipedia.org/wiki/Single_protein 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]. | ||
==Reference== | ==Reference== | ||
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[[Category: histone-like protein h1]] | [[Category: histone-like protein h1]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:03:05 2008'' | ||
Revision as of 14:03, 21 February 2008
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H-NS (DNA-BINDING DOMAIN)
OverviewOverview
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.
About this StructureAbout this Structure
1HNS is a Single protein structure of sequence from Escherichia coli. Full crystallographic 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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