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1hns

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[[Image:1hns.gif|left|200px]]
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{{STRUCTURE_1hns| PDB=1hns | SCENE= }}
{{STRUCTURE_1hns| PDB=1hns | SCENE= }}
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'''H-NS (DNA-BINDING DOMAIN)'''
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===H-NS (DNA-BINDING DOMAIN)===
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==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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(as it appears on PubMed at http://www.pubmed.gov), where 7875316 is the PubMed ID number.
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{{ABSTRACT_PUBMED_7875316}}
==About this Structure==
==About this Structure==
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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].
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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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:02:55 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:26:45 2008''

Revision as of 05:26, 1 July 2008

Image:1hns.png

Template:STRUCTURE 1hns

H-NS (DNA-BINDING DOMAIN)

Template:ABSTRACT PUBMED 7875316

About this Structure

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

Reference

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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