Unique structural and ligand-binding properties of the Staphylococcus aureus serine hydrolase FphE

Jo J, Upadhyay T, You X Bennett J, Lee H, Bogyo M, Fellner M, Proceedings of the National Academy of Sciences 123(13) (2026) DOI

SASDX74 – Carboxylic ester hydrolase FphF

S-formylglutathione hydrolase
MWexperimental 60 kDa
MWexpected 59 kDa
VPorod 99 nm3
log I(s) 1.32×10-2 1.32×10-3 1.32×10-4 1.32×10-5
S-formylglutathione hydrolase small angle scattering data  s, nm-1
ln I(s)
S-formylglutathione hydrolase Guinier plot ln 1.32×10-2 Rg: 2.8 nm 0 (2.8 nm)-2 s2
(sRg)2I(s)/I(0)
S-formylglutathione hydrolase Kratky plot 1.104 0 √3 sRg
p(r)
S-formylglutathione hydrolase pair distance distribution function Rg: 2.8 nm 0 Dmax: 9.3 nm

Data validation

Fits and models

log I(s)
 s, nm-1
S-formylglutathione hydrolase PDB (PROTEIN DATA BANK) model
log I(s)
 s, nm-1
S-formylglutathione hydrolase SREFLEX model
log I(s)
 s, nm-1
S-formylglutathione hydrolase DAMMIF model
Synchrotron SAXS data from solutions of carboxylic ester hydrolase FphF in 10 mM HEPES, 50 mM NaCl, 0.1% w/v NaN3, pH 7.5 were collected on the BioSAXS beam line at the Australian Synchrotron (Melbourne, Australia) using a Pilatus3 X 2M detector at a sample-detector distance of 2.5 m and at a wavelength of λ = 0.1 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Co-flow in-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 50.00 μl sample at 6.5 mg/ml was injected at a 0.40 ml/min flow rate onto a GE Superdex 75 Increase 5/150 column at 21°C. 641 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.

S-formylglutathione hydrolase
Mol. type   Protein
Organism   Staphylococcus aureus (strain USA300)
Olig. state   Dimer
Mon. MW   29.3 kDa
 
UniProt   A0A0H2XFN6 (1-253)
Sequence   FASTA
 
PDB ID   6VH9
 
PDB ID   6VH9