The role of conformational flexibility in Baeyer-Villiger monooxygenase catalysis and structure.

Yachnin BJ, Lau PCK, Berghuis AM, Biochim Biophys Acta 1864(12):1641-1648 (2016) Europe PMC

SASDBW5 – Cyclopentadecanone monooxygenase, NADP+ and cyclopentadecanone, wild-type

Cyclopentadecanone 1,2-monooxygenase
MWI(0) 72 kDa
MWexpected 68 kDa
VPorod 110 nm3
log I(s) 1.98×103 1.98×102 1.98×101 1.98×100
Cyclopentadecanone 1,2-monooxygenase small angle scattering data  s, nm-1
ln I(s)
Cyclopentadecanone 1,2-monooxygenase Guinier plot ln 1.99×103 Rg: 2.6 nm 0 (2.6 nm)-2 s2
(sRg)2I(s)/I(0)
Cyclopentadecanone 1,2-monooxygenase Kratky plot 1.104 0 3 sRg
p(r)
Cyclopentadecanone 1,2-monooxygenase pair distance distribution function Rg: 2.6 nm 0 Dmax: 9 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of Cyclopentadecanone monooxygenase, NADP+ and cyclopentadecanone, wild-type in 50mM Tris 2mM TCEP 5mM NADP+ 1mM cyclopentadecanon, pH 8 were collected on the 12.3.1 (SIBYLS) beam line at the Advanced Light Source (ALS) storage ring (Berkeley, CA, USA) using a MAR 165 CCD detector at a sample-detector distance of 1.5 m and at a wavelength of λ = 0.1 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 2.3 and 9 mg/ml were measured at 20°C. Four successive 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 concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.

Storage temperature = UNKNOWN. X-ray Exposure time = UNKNOWN

Cyclopentadecanone 1,2-monooxygenase
Mol. type   Protein
Organism   Pseudomonas sp. HI-70
Olig. state   Monomer
Mon. MW   69.1 kDa
 
UniProt   T2HVF7
Sequence   FASTA