Published March 21, 2008 | Version v1
Journal article

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

  • 1. Division of Structural Biology, Henry Wellcome Building for Genomic Medicine, University of Oxford, Roosevelt Drive, Oxford OX3 7BN (United Kingdom)
  • 2. The Oxford Protein Production Facility, Henry Wellcome Building for Genomic Medicine, University of Oxford, Roosevelt Drive, Oxford OX3 7BN (United Kingdom)
  • 3. Bacterial Pathogenesis and Functional Genomics Group, Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE (United Kingdom)

Description

The X-ray crystal structure of the cold-shock domain protein from N. meningitidis reveals a strand-exchanged dimer. 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

Availability note (English)

Available from http://dx.doi.org/10.1107/S1744309108005411; Available from http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2374261

Additional details

Publishing Information

Journal Title
Acta Crystallographica. Section F
Journal Volume
64
Journal Issue
Pt 4
Journal Page Range
p. 247-251
ISSN
1744-3091
CODEN
ACSFCL

INIS

Country of Publication
United Kingdom
Country of Input or Organization
International Atomic Energy Agency (IAEA)
INIS RN
46065807
Subject category
S75: CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY;
Descriptors DEI
CRYSTAL STRUCTURE; DIMERS; MATHEMATICAL SOLUTIONS; MONOMERS; PROTEINS; RESOLUTION; SOLUTIONS; STOICHIOMETRY
Descriptors DEC
DISPERSIONS; HOMOGENEOUS MIXTURES; MIXTURES; ORGANIC COMPOUNDS

Optional Information

Copyright
Copyright (c) International Union of Crystallography 2008
Notes
PMCID: PMC2374261; PMID: 18391418; PUBLISHER-ID: sw5023; OAI: oai:pubmedcentral.nih.gov:2374261