Please use this identifier to cite or link to this item: http://dl.umsu.ac.ir/handle/Hannan/11681
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
subject: Cold-shock domain proteins;Neisseria meningitidis;Domain-exchanged dimers
Year: 2008
Publisher: International Union of Crystallography
Description: Copyright @ 2008 International Union of Crystallography
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.
This study is funded by the UK Medical Research Council.
URI: http://onlinelibrary.wiley.com/doi/10.1107/S1744309108005411/abstract
http://bura.brunel.ac.uk/handle/2438/6647
http://dx.doi.org/10.1107/S1744309108005411
Standard no: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 64(Pt 4): 247 - 251, Apr 2008
1744-3091
Appears in Collections:Dept of Life Sciences Research Papers

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