Acyl chains stabilize the acylated domain and determine the receptor-mediated interaction of the Bordetella adenylate cyclase toxin with cell membrane.
Espinosa-Vinals C,
Stransky J,
Osicka R,
Osickova A,
Jurnecka D,
Sebo P,
Bumba L
J Biol Chem
:110392
(2025 Jun 19)
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Sample: |
Double-acylated variant of a genetic fusion comprising the C-terminal folding scaffold of RTX block V (residues 1562–1681 of CyaA) and the CyaA residues 719–1294 monomer, 78 kDa Bordetella pertussis protein
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Buffer: |
50 mM NaCl, 3 mM CaCl2, 20 mM Tris, pH: 8 |
Experiment: |
SAXS
data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2022 Feb 15
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RgGuinier |
3.4 |
nm |
Dmax |
14.5 |
nm |
VolumePorod |
67 |
nm3 |
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Sample: |
Mono-acylated variant of a genetic fusion comprising the C-terminal folding scaffold of RTX block V (residues 1562–1681 of CyaA) and the CyaA residues 719–1294 monomer, 78 kDa Bordetella pertussis protein
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Buffer: |
50 mM NaCl, 3 mM CaCl2, 20 mM Tris, pH: 8 |
Experiment: |
SAXS
data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2022 Feb 16
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RgGuinier |
5.0 |
nm |
Dmax |
25.8 |
nm |
VolumePorod |
178 |
nm3 |
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Sample: |
Mono-acylated variant of a genetic fusion comprising the C-terminal folding scaffold of RTX block V (residues 1562–1681 of CyaA) and the CyaA residues 719–1294 monomer, 78 kDa Bordetella pertussis protein
|
Buffer: |
50 mM NaCl, 3 mM CaCl2, 20 mM Tris, pH: 8 |
Experiment: |
SAXS
data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2022 Feb 17
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RgGuinier |
5.3 |
nm |
Dmax |
26.3 |
nm |
VolumePorod |
187 |
nm3 |
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Sample: |
Non-acylated variant of a genetic fusion comprising the C-terminal folding scaffold of RTX block V (residues 1562–1681 of CyaA) and the CyaA residues 719–1294 monomer, 78 kDa Bordetella pertussis protein
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Buffer: |
50 mM NaCl, 3 mM CaCl2, 20 mM Tris, pH: 8 |
Experiment: |
SAXS
data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2022 Feb 22
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RgGuinier |
4.2 |
nm |
Dmax |
17.8 |
nm |
VolumePorod |
133 |
nm3 |
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