1NI8

H-NS dimerization motif

Summary for 1NI8

• Entry DOI: 10.2210/pdb1ni8/pdb
• Descriptor: DNA-binding protein H-NS (1 entity in total)
• Functional Keywords: dimerization, protein-dna interaction, dna binding protein
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 10672.08

Authors

Bloch, V.,Yang, Y.,Margeat, E.,Chavanieu, A.,Aug, M.T.,Robert, B.,Arold, S.,Rimsky, S.,Kochoyan, M. (deposition date: 2002-12-22, release date: 2003-02-18, Last modification date: 2024-05-22)

Primary citation

Bloch, V.,Yang, Y.,Margeat, E.,Chavanieu, A.,Auge, M.T.,Robert, B.,Arold, S.,Rimsky, S.,Kochoyan, M.
The H-NS dimerisation domain defines a new fold contributing to DNA recognition
Nat.Struct.Biol., 10:3-, 2003

PubMed Abstract: 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.

PubMed: 12592399
DOI: 10.1038/nsb904

Experimental method

SOLUTION NMR