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Structure of the cold-shock domain protein from Neisseria meningitidis reveals a strand-exchanged dimer.

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.
Publication status:
Published

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Publisher copy:
10.1107/s1744309108005411

Authors


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Institution:
University of Oxford
Department:
Oxford, MSD, Pathology Dunn School
Role:
Author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Biology
Role:
Author
Journal:
Acta crystallographica. Section F, Structural biology and crystallization communications
Volume:
64
Issue:
Pt 4
Pages:
247-251
Publication date:
2008-04-05
DOI:
EISSN:
1744-3091
ISSN:
1744-3091
URN:
uuid:4873665a-d5d0-48a5-a66a-f81ec18d56f3
Source identifiers:
23135
Local pid:
pubs:23135

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