S. aureus Eap is a polyvalent inhibitor of neutrophil serine proteases.

Mishra N, Gido CD, Herdendorf TJ, Hammel M, Hura GL, Fu ZQ, Geisbrecht BV, J Biol Chem 300(9):107627 (2024) Europe PMC

SASDVF2 – Staphylococcal extracellular adherence protein (Eap) in unbound form

Protein map
MWI(0) 55 kDa
MWexpected 50 kDa
VPorod 64 nm3
log I(s) 5.31×101 5.31×100 5.31×10-1 5.31×10-2
Protein map small angle scattering data  s, nm-1
ln I(s)
Protein map Guinier plot ln 5.31×101 Rg: 4.0 nm 0 (4.0 nm)-2 s2
(sRg)2I(s)/I(0)
Protein map Kratky plot 1.104 0 √3 sRg

Data validation

Fits and models

log I(s)
 s, nm-1
Protein map MULTIFOXS model
log I(s)
 s, nm-1
Protein map MULTIFOXS model
Protein map MULTIFOXS model
log I(s)
 s, nm-1
Protein map MULTIFOXS model
Protein map MULTIFOXS model
Protein map MULTIFOXS model
Synchrotron SAXS data from solutions of Staphylococcal extracellular adherence protein (Eap) in unbound form in 20 mM HEPES, 140 mM NaCl, pH 7.4 were collected on the 12.3.1 (SIBYLS) beam line at the Advanced Light Source (ALS) storage ring (Berkeley, CA, USA) using a Pilatus3 X 2M detector at a sample-detector distance of 2.1 m and at a wavelength of λ = 0.1127 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 60.00 μl sample at 5 mg/ml was injected at a 0.65 ml/min flow rate onto a Shodex LW-803 column at 4°C. 660 successive 2 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.

Protein map (Eap)
Mol. type   Protein
Organism   Staphylococcus aureus (strain Mu50 / ATCC 700699)
Olig. state   Monomer
Mon. MW   50.3 kDa
 
UniProt   Q99QS1 (32-478)
Sequence   FASTA