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.
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.
Caria
S
S
Structural Biology Group, European Synchrotron Radiation Facility, France.
de Sanctis
D
D
Enguita
F J
FJ
McSweeney
S
S
D000255:Adenosine Triphosphate / Q000737:chemistry* / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D055162:Biocatalysis; D003460:Crystallization; D018360:Crystallography, X-Ray; D034301:Deinococcus / Q000201:enzymology*; D054730:Protein Interaction Domains and Motifs
D001426:Bacterial Proteins; C061279:PhoR protein, Bacteria; D000255:Adenosine Triphosphate
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