Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 64, Part 4 (April 2008)

structural genomics communications

Acta Cryst. (2008). F64, 247-251 [ doi:10.1107/S1744309108005411 ]

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

J. Ren, J. E. Nettleship, S. Sainsbury, N. J. Saunders and R. J. Owens

Abstract: 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 [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 µM.

PDB reference: 3cam

Keywords: cold-shock domain proteins; Neisseria meningitidis; domain-exchanged dimers.