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

SASDTU7 – Lactoferrin binding protein B (C-terminal alpha helical domain)

Transferrin-binding protein B
MWexperimental 35 kDa
MWexpected 32 kDa
VPorod 49 nm3
log I(s) 1.75×10-2 1.75×10-3 1.75×10-4 1.75×10-5
Transferrin-binding protein B small angle scattering data  s, nm-1
ln I(s)
Transferrin-binding protein B Guinier plot ln 1.75×10-2 Rg: 3.2 nm 0 (3.2 nm)-2 s2
(sRg)2I(s)/I(0)
Transferrin-binding protein B Kratky plot 1.104 0 √3 sRg
p(r)
Transferrin-binding protein B pair distance distribution function Rg: 3.5 nm 0 Dmax: 11.9 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) 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.

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