Methionine gamma lyase fused with S3 domain VGF forms octamers and adheres to tumor cells via binding EGFR

Bondarev N, Bagaeva D, Bazhenov S, Buben M, Bulushova N, Ryzhykau Y Okhrimenko I, Zagryadskaya Y, Maslov I, Anisimova N, Sokolova D, Kuklin A, Pokrovsky V, Manukhov I, Biochemical and Biophysical Research Communications :149319 (2023) DOI

SASDPQ5 – His-tagged L-methionine gamma-lyase from Clostridium tetani

L-methionine gamma-lyase
MWexperimental 211 kDa
MWexpected 181 kDa
VPorod 232 nm3
log I(s) 1.24×100 1.24×10-1 1.24×10-2 1.24×10-3
L-methionine gamma-lyase small angle scattering data  s, nm-1
ln I(s)
L-methionine gamma-lyase Guinier plot ln 1.24×100 Rg: 4.0 nm 0 (4.0 nm)-2 s2
(sRg)2I(s)/I(0)
L-methionine gamma-lyase Kratky plot 1.104 0 √3 sRg
p(r)
L-methionine gamma-lyase pair distance distribution function Rg: 4.0 nm 0 Dmax: 14.9 nm

Data validation

Fits and models

log I(s)
 s, nm-1
L-methionine gamma-lyase CHIMERA model
L-methionine gamma-lyase CHIMERA model
SANS data from solutions of His-tagged L-methionine gamma-lyase from Clostridium tetani in PBS-D2O (137 mM NaCl, 2.7 mM KCl, 10 mM Na2HPO4, 1.8 mM KH2PO4 (D2O buffer), pD 7.4) performed on the YuMO SANS TOF spectrometer (IBR-2: Frank Laboratory of Neutron Physics, Joint Institute for Nuclear Research; Dubna, Russian Federation) with a two He3-fulfilled, 8 independent wire detector system (sample-detector distances of 4.5 m and 12.97 m). The wavelengths used are from 0.05 to 0.8 nm, the contributions of which are separated using time-of-flight technology. One solute concentration of 10.00 mg/ml was measured at 20°C. 9000 successive 0.207 second frames were collected.

The protein of study is His-tagged L methionine gamma lyase from Clostridium tetani. The volume fractions of tetramers and octamers in solution are 37% and 63%, respectively.

L-methionine gamma-lyase (Ct-MGL)
Mol. type   Protein
Organism   Clostridium tetani
Olig. state   Tetramer
Mon. MW   45.4 kDa
 
UniProt   A0A1L7H888 (1-398)
Sequence   FASTA
 
PDB ID   5DX5
 
PDB ID   5DX5