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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.

Original publication

DOI

10.1107/S1744309108005411

Type

Journal article

Journal

Acta Crystallogr Sect F Struct Biol Cryst Commun

Publication Date

01/04/2008

Volume

64

Pages

247 - 251

Keywords

Amino Acid Sequence, Bacterial Proteins, Crystallography, X-Ray, Dimerization, Molecular Sequence Data, Neisseria meningitidis, Protein Binding, Protein Folding, Protein Structure, Tertiary