1ni8: Difference between revisions
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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.]] | ||
[[Category: | [[Category: Dimerization]] | ||
[[Category: | [[Category: Protein-dna interaction]] | ||
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Revision as of 23:34, 2 May 2008
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
