3CAM

Crystal structure of the cold shock domain protein from Neisseria meningitidis

Summary for 3CAM

• Entry DOI: 10.2210/pdb3cam/pdb
• Descriptor: Cold-shock domain family protein (2 entities in total)
• Functional Keywords: neisseria meningitidis, cold shock protein, chain swap, structural genomics, oxford protein production facility, oppf, gene regulation
• Biological source: Neisseria meningitidis MC58
• Cellular location: Cytoplasm : Q9JZZ4
• Total number of polymer chains: 2
• Total formula weight: 14593.75

Authors

Ren, J.,Sainsbury, S.,Owens, R.J.,Oxford Protein Production Facility (OPPF) (deposition date: 2008-02-20, release date: 2008-03-25, Last modification date: 2024-11-20)

Primary citation

Ren, J.,Nettleship, J.E.,Sainsbury, S.,Saunders, N.J.,Owens, R.J.
Structure of the cold-shock domain protein from Neisseria meningitidis reveals a strand-exchanged dimer.
Acta Crystallogr.,Sect.F, 64:247-251, 2008

PubMed Abstract: 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.

PubMed: 18391418
DOI: 10.1107/S1744309108005411

Experimental method

X-RAY DIFFRACTION (2.6 Å)