1ni8
From Proteopedia
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| - | [[Image:1ni8.gif|left|200px]] | + | [[Image:1ni8.gif|left|200px]] |
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| - | '''H-NS dimerization motif''' | + | {{Structure |
| + | |PDB= 1ni8 |SIZE=350|CAPTION= <scene name='initialview01'>1ni8</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= hns ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''H-NS dimerization motif''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1NI8 is a [ | + | 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]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12592399 12592399] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: protein-dna interaction]] | [[Category: protein-dna interaction]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:57:13 2008'' |
Revision as of 10:57, 20 March 2008
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| Gene: | hns (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 12:57:13 2008
