Structure of the cold-shock domain protein from Neisseria meningitidis reveals a strand-exchanged dimer.

Journal article

The structure of the cold-shock domain protein from Neisseria meningitidis has been solved to 2.6 A resolution and shown to comprise a dimer formed by the exchange of two beta-strands between protein monomers. The overall fold of the monomer closely resembles those of other bacterial cold-shock proteins. The neisserial protein behaved as a monomer in solution and was shown to bind to a hexathymidine oligonucleotide with a stoichiometry of 1:1 and a K(d) of 1.25 microM.

Authors: Ren, J; Nettleship, J; Sainsbury, S; Saunders, N; Owens, R

• Publication status: Published
• Journal: Acta crystallographica. Section F, Structural biology and crystallization communications
• Volume: 64
• Issue: Pt 4
• Pages: 247-251
• Publication date: 2008-04-01
• DOI: 10.1107/s1744309108005411
• EISSN: 1744-3091
• ISSN: 1744-3091
• Language: English
• Keywords: Amino Acid Sequence; Protein Binding; Bacterial Proteins; Protein Folding; Protein Structure, Tertiary; Crystallography, X-Ray; Dimerization; Neisseria meningitidis; Molecular Sequence Data