The structural basis of fungal glucuronoyl esterase activity on natural substrates.

Ernst HA, Mosbech C, Langkilde AE, Westh P, Meyer AS, Agger JW, Larsen S, Nat Commun 11(1):1026 (2020) Europe PMC

SASDGC6 – Glucuronoyl esterase, deglycolsylated full length

4-O-methyl-glucuronoyl methylesterase (Glucuronoyl esterase)
MWexperimental 45 kDa
MWexpected 51 kDa
VPorod 71 nm3
log I(s) 6.20×10-2 6.20×10-3 6.20×10-4 6.20×10-5
4-O-methyl-glucuronoyl methylesterase (Glucuronoyl esterase) small angle scattering data  s, nm-1
ln I(s)
4-O-methyl-glucuronoyl methylesterase (Glucuronoyl esterase) Guinier plot ln 6.20×10-2 Rg: 3.2 nm 0 (3.2 nm)-2 s2
(sRg)2I(s)/I(0)
4-O-methyl-glucuronoyl methylesterase (Glucuronoyl esterase) Kratky plot 1.104 0 √3 sRg
p(r)
4-O-methyl-glucuronoyl methylesterase (Glucuronoyl esterase) pair distance distribution function Rg: 3.2 nm 0 Dmax: 11 nm

Data validation

Fits and models

log I(s)
 s, nm-1
4-O-methyl-glucuronoyl methylesterase (Glucuronoyl esterase) DAMMIN model
log I(s)
 s, nm-1
4-O-methyl-glucuronoyl methylesterase (Glucuronoyl esterase) GASBOR model
SAXS data from solutions of full-length deglycolsylated glucuronoyl esterase in 20 mM sodium acetate, pH 5 were collected using a Xenocs BioXolver L with GeniX3D (University of Copenhagen, Department of Drug Design and Pharmacology) equipped with a Pilatus3 R 300K detector at a sample-detector distance of 0.6 m and at a wavelength of λ = 0.154 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 21°C. 10 successive 60 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.

4-O-methyl-glucuronoyl methylesterase (Glucuronoyl esterase) (CuGE)
Mol. type   Protein
Organism   Cerrena unicolor
Olig. state   Monomer
Mon. MW   50.9 kDa
 
UniProt   A0A0A7EQR3 (18-474)
Sequence   FASTA