Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 14-Day Trial for You or Your Team.

Learn More →

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

Structure of the cold‐shock domain protein from Neisseria meningitidis reveals a strand‐exchanged... 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 β‐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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

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

Loading next page...
 
/lp/wiley/structure-of-the-cold-shock-domain-protein-from-neisseria-meningitidis-nWp0X5cf1i

References (29)

Publisher
Wiley
Copyright
Copyright © 2008 Wiley Subscription Services, Inc., A Wiley Company
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S1744309108005411
pmid
18391418
Publisher site
See Article on Publisher Site

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 β‐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.

Journal

Acta Crystallographica Section FWiley

Published: Apr 1, 2008

There are no references for this article.