Legionella pneumophila macrophage infectivity potentiator protein appendage domains modulate protein dynamics and inhibitor binding

Wiedemann C, Whittaker J, Carrillo V, Goretzki B Dajka M, Tebbe F, Harder J, Krajczy P, Joseph B, Hausch F, Guskov A, Hellmich U, International Journal of Biological Macromolecules :126366 (2023) DOI

SASDSY6 – Outer membrane protein MIP (LpMIP) apo state

Outer membrane protein MIP
MWI(0) 41 kDa
MWexpected 46 kDa
VPorod 66 nm3
log I(s) 8.49×103 8.49×102 8.49×101 8.49×100
Outer membrane protein MIP small angle scattering data  s, nm-1
ln I(s)
Outer membrane protein MIP Guinier plot ln 8.49×103 Rg: 3.1 nm 0 (3.1 nm)-2 s2
(sRg)2I(s)/I(0)
Outer membrane protein MIP Kratky plot 1.104 0 √3 sRg
p(r)
Outer membrane protein MIP pair distance distribution function Rg: 3.2 nm 0 Dmax: 10.0 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Outer membrane protein MIP SREFLEX model
Synchrotron SAXS data from solutions of outer membrane protein MIP (LpMIP) in 20 mM Tris-HCl, 150 mM NaCl, 10 mM DTT, pH 7.5 were collected on the EMBL P12 beam line at PETRA III (DESY; 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). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 45.00 μl sample at 10 mg/ml was injected at a 0.30 ml/min flow rate onto a GE Superdex 200 Increase 5/150 column at 20°C. 2400 successive 0.250 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.

Outer membrane protein MIP (LpMIP)
Mol. type   Protein
Organism   Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Olig. state   Dimer
Mon. MW   22.8 kDa
 
UniProt   Q5ZXE0 (21-233)
Sequence   FASTA
 
PDB ID   1FD9