1ni8

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{{STRUCTURE_1ni8| PDB=1ni8 | SCENE= }}
{{STRUCTURE_1ni8| PDB=1ni8 | SCENE= }}
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'''H-NS dimerization motif'''
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===H-NS dimerization motif===
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==Overview==
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H-NS, a protein found in Gram-negative bacteria, is involved in structuring the bacterial chromosome and acts as a global regulator for the expression of a wide variety of genes. These functions are correlated with both its DNA-binding and oligomerization properties. We have identified the minimal dimerization domain of H-NS, a 46 amino acid-long N-terminal fragment, and determined its structure using heteronuclear NMR spectroscopy. The highly intertwined structure of the dimer, reminiscent of a handshake, defines a new structural fold, which may offer a possibility for discriminating prokaryotic from eukaryotic proteins in drug design. Using mutational analysis, we also show that this N-terminal domain actively contributes to DNA binding, conversely to the current paradigm. Together, our data allows us to propose a model for the action of full length H-NS.
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{{ABSTRACT_PUBMED_12592399}}
==About this Structure==
==About this Structure==
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1NI8 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=1NI8 OCA].
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1NI8 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=1NI8 OCA].
==Reference==
==Reference==
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[[Category: Dimerization]]
[[Category: Dimerization]]
[[Category: Protein-dna interaction]]
[[Category: Protein-dna interaction]]
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Revision as of 14:14, 28 July 2008

Image:1ni8.png

Template:STRUCTURE 1ni8

H-NS dimerization motif

Template:ABSTRACT PUBMED 12592399

About this Structure

1NI8 is a Single protein structure of sequence from Escherichia coli. Full experimental information is available from OCA.

Reference

The H-NS dimerization domain defines a new fold contributing to DNA recognition., Bloch V, Yang Y, Margeat E, Chavanieu A, Auge MT, Robert B, Arold S, Rimsky S, Kochoyan M, Nat Struct Biol. 2003 Mar;10(3):212-8. PMID:12592399

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