The structure of the KinA-Sda complex suggests an allosteric mechanism of histidine kinase inhibition.

Whitten AE, Jacques DA, Hammouda B, Hanley T, King GF, Guss JM, Trewhella J, Langley DB, J Mol Biol 368(2):407-20 (2007) Europe PMC

SASDHZ3 – Sporulation kinase A

Sporulation kinase A
MWI(0) 52 kDa
MWexpected 51 kDa
VPorod 76 nm3
log I(s) 1.72×102 1.72×101 1.72×100 1.72×10-1
Sporulation kinase A small angle scattering data  s, nm-1
ln I(s)
Sporulation kinase A Guinier plot ln 1.73×102 Rg: 2.9 nm 0 (2.9 nm)-2 s2
Sporulation kinase A Kratky plot 1.104 0 3 sRg
Sporulation kinase A pair distance distribution function Rg: 3.0 nm 0 Dmax: 9.5 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Sporulation kinase A SASREF model

SAXS data from solutions of Sporulation kinase A in 50mM Tris, 200mM NaCl, 150mM Imidazole, pH 8.5 were collected using a Bruker Hi-Star detector at a sample-detector distance of 65 m and at a wavelength of λ = 0.15418 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 3.70 mg/ml was measured at 20°C. Three successive 3600 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

X-ray scattering data from the from the autokinase domain of the histidine kinase KinA in 50 mM Tris-HCl 200 mM NaCl 150 mM imidazole pH 8.5 were collected on a Bruker Nanostar instrument at the Bragg Institute (Australian Nuclear Science and Technology Organisation, Lucas Heights, Australia) using a HiStar 2D detector (I(s) vs s, where s = 4π sin θ/λ and 2θ is the scattering angle; λ=0.15406 nm). Approximately 15 µL of a 3.7 mg/ml protein solution was loaded into a quartz capillary mounted in a stainless steel holder. Three sucessive 3600s second frames were collected, and the buffer was collected in an analogous fashion. The data were radially averaged, and the scattering of the solvent-blank was subtracted. The data are on an arbitrary scale, and the mass of the protein was determined using a lysozyme secondary standard at a concentration of 17.5 mg/ml. The model and corresponding fits include are derived from a rigid body model using SASREF.

Sporulation kinase A (KinA)
Mol. type   Protein
Organism   Bacillus subtilis
Olig. state   Dimer
Mon. MW   25.4 kDa
UniProt   P16497 (383-606)
Sequence   FASTA