Almost half of the RTX domain is dispensable for complement receptor 3 binding and cell-invasive activity of the adenylate cyclase toxin.

Espinosa-Vinals CA, Masin J, Holubova J, Stanek O, Jurnecka D, Osicka R, Sebo P, Bumba L
J Biol Chem :100833 (2021 May 26)
PMID: 34051233
doi: 10.1016/j.jbc.2021.100833 		Submitted to SASBDB: 2021 Mar 15
Published in SASBDB:

SASDL62 – The truncated RTX domain of adenylate cyclase toxin CyaA - construct RTX-1 (amino acids 1132-1294 and 1562-1681 of CyaA)

hybrid RTX-1 construct (amino acids 1132-1294 and 1562-1681 of CyaA) experimental SAS data
DAMFILT model
Sample: Hybrid RTX-1 construct (amino acids 1132-1294 and 1562-1681 of CyaA) monomer, 30 kDa Bordetella pertussis protein
Buffer: 10 mM Tris HCl, 150 mM NaCl, 10 mM CaClâ‚‚, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Dec 1
RgGuinier 2.4 nm
Dmax 8.2 nm
VolumePorod 41 nm3

SASDL72 – The truncated RTX domain of adenylate cyclase toxin CyaA - construct RTX-2 (amino acids 1132-1303 and 1562-1681 of CyaA)

hybrid RTX-2 construct (amino acids 1132-1303 and 1562-1681 of CyaA) experimental SAS data
DAMMIF model
Sample: Hybrid RTX-2 construct (amino acids 1132-1303 and 1562-1681 of CyaA) monomer, 31 kDa Bordetella pertussis protein
Buffer: 10 mM Tris HCl, 150 mM NaCl, 10 mM CaClâ‚‚, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Dec 1
RgGuinier 2.3 nm
Dmax 8.0 nm
VolumePorod 37 nm3