Structure of the cold-shock domain protein from Neisseria meningitidis reveals a strand-exchanged dimer
Acta Crystallographica Section F
Volume 64, Issue 4, pages 247–251, April 2008
How to Cite
Ren, J., Nettleship, J. E., Sainsbury, S., Saunders, N. J. and Owens, R. J. (2008), Structure of the cold-shock domain protein from Neisseria meningitidis reveals a strand-exchanged dimer. Acta Cryst. F, 64: 247–251. doi: 10.1107/S1744309108005411
- cold-shock domain proteins;
- Neisseria meningitidis;
- domain-exchanged dimers.
The structure of the cold-shock domain protein from Neisseria meningitidis has been solved to 2.6 Å resolution and shown to comprise a dimer formed by the exchange of two β-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 Kd of 1.25 µM.