Please use this identifier to cite or link to this item:
|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|
|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.
|Standard no:||Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 64(Pt 4): 247 - 251, Apr 2008|
|Appears in Collections:||Dept of Life Sciences Research Papers|
Files in This Item:
Click on the URI links for accessing contents.
Items in HannanDL are protected by copyright, with all rights reserved, unless otherwise indicated.