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PDBsum entry 3cam

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protein Protein-protein interface(s) links
Gene regulation PDB id
3cam
Jmol
Contents
Protein chains
67 a.a. *
Waters ×16
* Residue conservation analysis
PDB id:
3cam
Name: Gene regulation
Title: Crystal structure of the cold shock domain protein from neis meningitidis
Structure: Cold-shock domain family protein. Chain: a, b. Engineered: yes
Source: Neisseria meningitidis mc58. Organism_taxid: 122586. Strain: mc58 / serogroup b. Gene: nmb0838. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.60Å     R-factor:   0.236     R-free:   0.297
Authors: J.Ren,S.Sainsbury,R.J.Owens,Oxford Protein Production Facili
Key ref: J.Ren et al. (2008). Structure of the cold-shock domain protein from Neisseria meningitidis reveals a strand-exchanged dimer. Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 247-251. PubMed id: 18391418
Date:
20-Feb-08     Release date:   25-Mar-08    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9JZZ4  (Q9JZZ4_NEIMB) -  Cold-shock domain family protein
Seq:
Struc:
67 a.a.
67 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     transcription, DNA-dependent   2 terms 
  Biochemical function     nucleic acid binding     2 terms  

 

 
Acta Crystallogr Sect F Struct Biol Cryst Commun 64:247-251 (2008)
PubMed id: 18391418  
 
 
Structure of the cold-shock domain protein from Neisseria meningitidis reveals a strand-exchanged dimer.
J.Ren, J.E.Nettleship, S.Sainsbury, N.J.Saunders, R.J.Owens.
 
  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.