Structure and catalytic mechanism of the evolutionarily unique bacterial chalcone isomerase.

Thomsen M, Tuukkanen A, Dickerhoff J, Palm GJ, Kratzat H, Svergun DI, Weisz K, Bornscheuer UT, Hinrichs W, Acta Crystallogr D Biol Crystallogr 71(Pt 4):907-17 (2015) Europe PMC

SASDAM6 – Naringenin-bound chalcone isomerase

Chalcone isomerase with Naringenin
MWI(0) 190 kDa
MWexpected 194 kDa
VPorod 320 nm3
log I(s) 2.53×104 2.53×103 2.53×102 2.53×101
Chalcone isomerase with Naringenin small angle scattering data  s, nm-1
ln I(s)
Chalcone isomerase with Naringenin Guinier plot ln 2.53×104 Rg: 3.7 nm 0 (3.7 nm)-2 s2
(sRg)2I(s)/I(0)
Chalcone isomerase with Naringenin Kratky plot 1.104 0 √3 sRg
p(r)
Chalcone isomerase with Naringenin pair distance distribution function Rg: 3.6 nm 0 Dmax: 11 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of Naringenin-bound chalcone isomerase in 50 mM sodium phosphate, pH 6.8 were collected on the EMBL P12 beam line at the PETRA III storage ring (DESY; Hamburg, Germany) using a Pilatus 2M detector at a sample-detector distance of 3.1 m and at a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.8 and 2.6 mg/ml were measured at 10°C. 20 successive 0.050 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. The low angle data collected at lower concentrations were extrapolated to infinite dilution and merged with the higher concentration data to yield the final composite scattering curve.

Concentrations used: 13.5 µM CHI, 1 mM naringenin.

Chalcone isomerase with Naringenin (naringenin-CHI)
Mol. type   Protein
Organism   Eubacterium ramulus
Olig. state   Hexamer
Mon. MW   32.4 kDa
 
UniProt   V9P0A9
Sequence   FASTA