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

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 prot...

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Détails bibliographiques
Auteurs principaux: Ren, J, Nettleship, J, Sainsbury, S, Saunders, N, Owens, R
Format: Journal article
Langue:English
Publié: 2008
Description
Résumé: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.