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