Structural basis of cell surface signaling by a conserved sigma regulator in Gram-negative bacteria.

Jensen JL, Jernberg BD, Sinha S, Colbert CL, J Biol Chem (2020) Europe PMC

SASDGA5 – The C-terminal cell-surface signaling domain of the Pseudomonas capeferrum anti-sigma regulator PupR

PupR protein
MWexperimental 26 kDa
MWexpected 24 kDa
VPorod 49 nm3
log I(s) 1.76×101 1.76×100 1.76×10-1 1.76×10-2
PupR protein small angle scattering data  s, nm-1
ln I(s)
PupR protein Guinier plot ln 1.76×101 Rg: 2.2 nm 0 (2.2 nm)-2 s2
(sRg)2I(s)/I(0)
PupR protein Kratky plot 1.104 0 √3 sRg
p(r)
PupR protein pair distance distribution function Rg: 2.2 nm 0 Dmax: 7.5 nm

Data validation

Fits and models

log I(s)
 s, nm-1
PupR protein MULTIFOXS model
log I(s)
 s, nm-1
PupR protein OTHER model
log I(s)
 s, nm-1
PupR protein DAMFILT model
Synchrotron SAXS data from solutions of the C-terminal cell-surface signaling domain of PupR in 25 mM HEPES 400 mM LiCl 10% v/v glycerol, pH 7.5 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 3.5 m and at a wavelength of λ = 0.103 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 500.00 μl sample at 9.6 mg/ml was injected at a 0.60 ml/min flow rate onto a GE Superdex 200 Increase 10/300 column at 25°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of an appropriate solvent-blank was subtracted from the SEC elution peak of the sample.

Storage temperature = UNKNOWN. X-ray Exposure time = UNKNOWN. Number of frames = UNKNOWN

PupR protein (PupR)
Mol. type   Protein
Organism   Pseudomonas putida
Olig. state   Monomer
Mon. MW   24.1 kDa
 
UniProt   Q52209 (110-324)
Sequence   FASTA