3cam | pdb_00003cam
From Proteopedia
Crystal structure of the cold shock domain protein from Neisseria meningitidis
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Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. Structure of the cold-shock domain protein from Neisseria meningitidis reveals a strand-exchanged dimer.,Ren J, Nettleship JE, Sainsbury S, Saunders NJ, Owens RJ Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Apr 1;64(Pt, 4):247-51. Epub 2008 Mar 21. PMID:18391418[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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