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 Jan 13)
PMID: 28084396
doi: 10.1038/srep40408
Submitted to SASBDB: 2016 Apr 5
Published in SASBDB:

SASDBP4 – Neisseria meningitidis iron-regulated outer membrane lipoprotein FrpD

Iron-regulated outer membrane lipoprotein FrpD experimental SAS data
DAMMIN model
Sample: Iron-regulated outer membrane lipoprotein FrpD monomer, 27 kDa Neisseria meningitidis protein
Buffer: 10 mM Tris-HCl 150 mM NaCl 0.01% NaN3, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Oct 19
RgGuinier 2.2 nm
Dmax 6.5 nm
VolumePorod 41 nm3

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

Iron-regulated outer membrane lipoprotein FrpDIron-regulated protein FrpC experimental SAS data
DAMMIN model
Sample: Iron-regulated outer membrane lipoprotein FrpD monomer, 27 kDa Neisseria meningitidis protein
Iron-regulated protein FrpC monomer, 46 kDa Neisseria meningitidis protein
Buffer: 50 mM Tris-HCl 150 mM NaCl 0.01% NaN3, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Oct 19
RgGuinier 3.7 nm
Dmax 13.5 nm
VolumePorod 123 nm3