1ni8
From Proteopedia
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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
Page seeded by OCA on Tue Nov 20 22:16:49 2007
