A secreted bacterial protein protects bacteria from cationic antimicrobial peptides by entrapment in phase separated droplets

Ostan N, Cole G, Wang F, Reichheld S, Moore G, Pan C, Yu R, Lai C, Sharpe S, Lee H, Schryvers A, Moraes T, PNAS Nexus (2024) DOI

SASDTV7 – Lactoferrin binding protein B (C-terminal alpha helical domain) bound to bovine lactoferrin

Lactoferrin
Transferrin-binding protein B
MWexperimental 186 kDa
MWexpected 107 kDa
VPorod 318 nm3
log I(s) 1.77×100 1.77×10-1 1.77×10-2 1.77×10-3
Lactoferrin Transferrin-binding protein B small angle scattering data  s, nm-1
ln I(s)
Lactoferrin Transferrin-binding protein B Guinier plot ln 1.78×100 Rg: 5.6 nm 0 (5.6 nm)-2 s2
(sRg)2I(s)/I(0)
Lactoferrin Transferrin-binding protein B Kratky plot 1.104 0 √3 sRg
p(r)
Lactoferrin Transferrin-binding protein B pair distance distribution function Rg: 5.8 nm 0 Dmax: 20.3 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of lactoferrin binding protein B (C-terminal alpha helical domain) bound to lactoferrin in 20 mM HEPES, 150 mM NaCl, pH 7.4 were collected on the BioCAT 18ID beam line at the Advanced Photon Source (APS), Argonne National Laboratory (Lemont, IL, USA) using a Pilatus3 X 1M detector at a sample-detector distance of 3.6 m and at a wavelength of λ = 0.1033 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 0.60 mg/ml was measured at 22°C. 1800 successive 0.500 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.

Lactoferrin (Lf)
Mol. type   Protein
Organism   Bos taurus
Olig. state   Monomer
Mon. MW   75.2 kDa
 
UniProt   Q6LBN7 (1-681)
Sequence   FASTA
 
Transferrin-binding protein B (LbpB-CαHD)
Mol. type   Protein
Organism   Moraxella bovis
Olig. state   Monomer
Mon. MW   31.7 kDa
 
UniProt   K7P8F3 (464-725)
Sequence   FASTA