Crystallization and preliminary X-ray characterization of a catalytic and ATP-binding domain of a putative PhoR histidine kinase from the gamma-radioresistant bacterium Deinococcus radiodurans

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Apr 1;66(Pt 4):401-4. doi: 10.1107/S1744309109054220. Epub 2010 Mar 31.

Abstract

The gene product of histidine kinase DR2244 (putative phoR) encoded by Deinococcus radiodurans has been suggested to be involved in the PhoR-PhoB two-component regulatory system. This two-component signalling system is activated upon phosphate starvation in several bacteria, including D. radiodurans. Single crystals were obtained from a recombinant preparation of the catalytic/ATP-binding (CA) domain of D. radiodurans PhoR (79-224) overexpressed in Escherichia coli. The crystals belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 46.9, b = 81.8, c = 204.6 A. The crystals contained six molecules in the asymmetric unit. Diffraction data were collected to 2.4 A resolution on beamline ID23-2 of the European Synchrotron Radiation Facility.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / chemistry*
  • Adenosine Triphosphate / metabolism
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Biocatalysis*
  • Crystallization
  • Crystallography, X-Ray
  • Deinococcus / enzymology*
  • Protein Interaction Domains and Motifs*

Substances

  • Bacterial Proteins
  • PhoR protein, Bacteria
  • Adenosine Triphosphate