1ni8

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[[Image:1ni8.gif|left|200px]]
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{{Structure
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|GENE= hns ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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{{STRUCTURE_1ni8| PDB=1ni8 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ni8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ni8 OCA], [http://www.ebi.ac.uk/pdbsum/1ni8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ni8 RCSB]</span>
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'''H-NS dimerization motif'''
'''H-NS dimerization motif'''
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[[Category: Robert, B.]]
[[Category: Robert, B.]]
[[Category: Yang, Y.]]
[[Category: Yang, Y.]]
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[[Category: dimerization]]
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[[Category: Dimerization]]
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[[Category: protein-dna interaction]]
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[[Category: Protein-dna interaction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:30:44 2008''
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Revision as of 23:34, 2 May 2008

Template:STRUCTURE 1ni8

H-NS dimerization motif


Overview

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.

About this Structure

1NI8 is a Single protein structure of sequence from Escherichia coli. Full crystallographic 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 Page seeded by OCA on Sat May 3 02:34:00 2008

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