Structural basis of the interaction between the putative adhesion-involved and iron-regulated FrpD and FrpC proteins of Neisseria meningitidis.

Sviridova E, Rezacova P, Bondar A, Veverka V, Novak P, Schenk G, Svergun DI, Kuta Smatanova I, Bumba L, Sci Rep 7:40408 (2017) Europe PMC

SASDBQ4 – Neisseria meningitidis iron-regulated FrpD-FrpC lipoprotein/protein complex

Iron-regulated outer membrane lipoprotein FrpD
Iron-regulated protein FrpC
MWexperimental 40 kDa
MWexpected 73 kDa
VPorod 123 nm3
log I(s) 5.03×101 5.03×100 5.03×10-1 5.03×10-2
Iron-regulated outer membrane lipoprotein FrpD Iron-regulated protein FrpC small angle scattering data  s, nm-1
ln I(s)
Iron-regulated outer membrane lipoprotein FrpD Iron-regulated protein FrpC Guinier plot ln 5.03×101 Rg: 3.7 nm 0 (3.7 nm)-2 s2
(sRg)2I(s)/I(0)
Iron-regulated outer membrane lipoprotein FrpD Iron-regulated protein FrpC Kratky plot 1.104 0 3 sRg
p(r)
Iron-regulated outer membrane lipoprotein FrpD Iron-regulated protein FrpC pair distance distribution function Rg: 3.9 nm 0 Dmax: 13.5 nm

Data validation


Fits and models


log I(s)
 s, nm-1
Iron-regulated outer membrane lipoprotein FrpD Iron-regulated protein FrpC DAMMIN model

X-ray synchrotron radiation scattering data from solutions of the 1:1 FrpD-FrpC complex from Neisseria meningitidis in 50 Tris-HCl, 150 mM NaCl, 0.01% NaN3 were collected on the X33 beam line at the DORIS storage ring (DESY, Hamburg, Germany) using a Pilatus 1M-W detector (I(s) vs s; s = 4π sin θ/λ, where 2θ is the scattering angle and λ=0.15 nm). The data displayed in this entry shows the merged and extrapolated to zero-concentration SAXS profile derived from solute concentrations measured across the range of 0.75-4.90 mg/ml. The SAXS data for each sample were measured using an exposure time of 120 s (collected as 8 x 15 s frames) and were normalized to the intensity of the transmitted beam and radially averaged. The scattering of the solvent-blank was subtracted and the resulting subtracted data were scaled to each respective protein concentration prior to merging.

Cell temperature = UNKNOWN

Tags: X33
Iron-regulated outer membrane lipoprotein FrpD (FrpD)
Mol. type   Protein
Organism   Neisseria meningitidis
Olig. state   Monomer
Mon. MW   26.8 kDa
 
UniProt   Q08840 (43-271)
Sequence   FASTA
 
Iron-regulated protein FrpC (FrpC)
Mol. type   Protein
Organism   Neisseria meningitidis
Olig. state   Monomer
Mon. MW   46.4 kDa
 
UniProt   Q9JYV5 (1-414)
Sequence   FASTA