Dimerization of the plant molybdenum insertase Cnx1E is required for synthesis of the molybdenum cofactor.

Krausze J, Probst C, Curth U, Reichelt J, Saha S, Schafflick D, Heinz DW, Mendel RR, Kruse T, Biochem J 474(1):163-178 (2017) Europe PMC

SASDCM8 – Mo-insertase domain Cnx1E from Arabidopsis thaliana

Molybdopterin biosynthesis protein CNX1
MWexperimental 99 kDa
MWexpected 99 kDa
VPorod 181 nm3
log I(s) 6.89×101 6.89×100 6.89×10-1 6.89×10-2
Molybdopterin biosynthesis protein CNX1 small angle scattering data  s, nm-1
ln I(s)
Molybdopterin biosynthesis protein CNX1 Guinier plot ln 6.90×101 Rg: 3.6 nm 0 (3.6 nm)-2 s2
(sRg)2I(s)/I(0)
Molybdopterin biosynthesis protein CNX1 Kratky plot 1.104 0 √3 sRg
p(r)
Molybdopterin biosynthesis protein CNX1 pair distance distribution function Rg: 3.8 nm 0 Dmax: 15 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Molybdopterin biosynthesis protein CNX1 PDB (PROTEIN DATA BANK) model
Synchrotron SAXS data from solutions of Mo-insertase domain Cnx1E from Arabidopsis thaliana in 20 mM Hepes/KOH, 150 mM NaCl, 1 mM EDTA, 2 % (v/v) glycerol, pH 7.4 were collected on the ID14-3 beam line at the ESRF storage ring (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.09919 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1.7 and 12.5 mg/ml were measured at 20°C. 10 successive 1 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 concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.

Molybdopterin biosynthesis protein CNX1 (Cnx1E)
Mol. type   Protein
Organism   Arabidopsis thaliana
Olig. state   Dimer
Mon. MW   49.7 kDa
 
UniProt   Q39054 (1-451)
Sequence   FASTA
 
PDB ID   5G2R