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http://bura.brunel.ac.uk/handle/2438/6647
Title: | Structure of the cold-shock domain protein from Neisseria meningitidis reveals a strand-exchanged dimer |
Authors: | Ren, J Nettleship, JE Sainsbury, S Saunders, NJ Owens, RJ |
Keywords: | Cold-shock domain proteins;Neisseria meningitidis;Domain-exchanged dimers |
Issue Date: | 2008 |
Publisher: | International Union of Crystallography |
Citation: | Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 64(Pt 4): 247 - 251, Apr 2008 |
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 -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. |
Description: | Copyright @ 2008 International Union of Crystallography |
URI: | http://onlinelibrary.wiley.com/doi/10.1107/S1744309108005411/abstract http://bura.brunel.ac.uk/handle/2438/6647 |
DOI: | http://dx.doi.org/10.1107/S1744309108005411 |
ISSN: | 1744-3091 |
Appears in Collections: | Biological Sciences Publications Dept of Life Sciences Research Papers |
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