1ni8
From Proteopedia
(New page: 200px<br /><applet load="1ni8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ni8" /> '''H-NS dimerization motif'''<br /> ==Overview...) |
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| - | [[Image:1ni8.gif|left|200px]]<br /><applet load="1ni8" size=" | + | [[Image:1ni8.gif|left|200px]]<br /><applet load="1ni8" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ni8" /> | caption="1ni8" /> | ||
'''H-NS dimerization motif'''<br /> | '''H-NS dimerization motif'''<br /> | ||
==Overview== | ==Overview== | ||
| - | H-NS, a protein found in Gram-negative bacteria, is involved in | + | 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== | ==About this Structure== | ||
| - | 1NI8 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:// | + | 1NI8 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=1NI8 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Arold, S.]] | [[Category: Arold, S.]] | ||
| - | [[Category: Aug, M | + | [[Category: Aug, M T.]] |
[[Category: Bloch, V.]] | [[Category: Bloch, V.]] | ||
[[Category: Chavanieu, A.]] | [[Category: Chavanieu, A.]] | ||
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[[Category: protein-dna interaction]] | [[Category: protein-dna interaction]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:06:21 2008'' |
Revision as of 12:06, 21 February 2008
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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
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