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 Feb 26)
PMID: 32107313
doi: 10.1074/jbc.RA119.010697 		Submitted to SASBDB: 2019 Sep 16
Published in SASBDB:

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

PupR protein experimental SAS data
MULTIFOXS model
Sample: PupR protein monomer, 24 kDa Pseudomonas putida protein
Buffer: 25 mM HEPES 400 mM LiCl 10% v/v glycerol, pH: 7.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2016 Mar 16
RgGuinier 2.2 nm
Dmax 7.5 nm
VolumePorod 49 nm3

SASDGU5 – The C-terminal cell-surface signaling domain of the Pseudomonas capeferrum anti-sigma regulator PupR in complex with the outer membrane transporter PupB N-terminal signaling domain

PupR proteinFerric-pseudobactin BN7/BN8 receptor experimental SAS data
DAMFILT model
Sample: PupR protein monomer, 24 kDa Pseudomonas putida protein
Ferric-pseudobactin BN7/BN8 receptor monomer, 8 kDa Pseudomonas putida protein
Buffer: 25 mM HEPES 400 mM LiCl 10% v/v glycerol, pH: 7.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2016 Mar 16
RgGuinier 2.5 nm
Dmax 8.7 nm
VolumePorod 56 nm3