NMR structure of emfourin, a novel protein metalloprotease inhibitor: insights into the mechanism of action.

Bozin T, Berdyshev I, Chukhontseva K, Karaseva M, Konarev P, Varizhuk A, Lesovoy D, Arseniev A, Kostrov S, Bocharov E, Demidyuk I, J Biol Chem :104585 (2023) Europe PMC

SASDHN7 – Emfourin (M4in) from Serratia proteamaculans, M4 family peptidase inhibitor

Emfourin (Protealysin-associated protein)
MWI(0) 11 kDa
MWexpected 13 kDa
VPorod 16 nm3
log I(s) 6.98×101 6.98×100 6.98×10-1 6.98×10-2
Emfourin (Protealysin-associated protein) small angle scattering data  s, nm-1
ln I(s)
Emfourin (Protealysin-associated protein) Guinier plot ln 6.99×101 Rg: 1.7 nm 0 (1.7 nm)-2 s2
(sRg)2I(s)/I(0)
Emfourin (Protealysin-associated protein) Kratky plot 1.104 0 √3 sRg
p(r)
Emfourin (Protealysin-associated protein) pair distance distribution function Rg: 1.7 nm 0 Dmax: 5.5 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Emfourin (Protealysin-associated protein) DAMFILT model
Synchrotron SAXS data from solutions of Emfourin (M4in) in 50 mM Tris-HCL, pH 7.4 were collected on the EMBL P12 beam line at PETRA III (Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 2.00 mg/ml was measured at 20°C. 20 successive 0.050 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.

Emfourin (Protealysin-associated protein) (M4in)
Mol. type   Protein
Organism   Serratia proteamaculans
Olig. state   Monomer
Mon. MW   12.7 kDa
 
UniProt   A0A1X9WII3 (1-113)
Sequence   FASTA