+Open data
-Basic information
Entry | Database: SASBDB / ID: SASDB84 |
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Sample | CyaA Block V
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Function / homology | Function and homology information calcium- and calmodulin-responsive adenylate cyclase activity / hemolysis in another organism / adenylate cyclase / cAMP biosynthetic process / adenylate cyclase activity / channel activity / toxin activity / positive regulation of cytosolic calcium ion concentration / calmodulin binding / calcium ion binding ...calcium- and calmodulin-responsive adenylate cyclase activity / hemolysis in another organism / adenylate cyclase / cAMP biosynthetic process / adenylate cyclase activity / channel activity / toxin activity / positive regulation of cytosolic calcium ion concentration / calmodulin binding / calcium ion binding / host cell plasma membrane / extracellular region / ATP binding / membrane Similarity search - Function |
Biological species | Bordetella pertussis (bacteria) |
Citation | Journal: Mol Cell / Year: 2016 Title: Calcium-Driven Folding of RTX Domain β-Rolls Ratchets Translocation of RTX Proteins through Type I Secretion Ducts. Authors: Ladislav Bumba / Jiri Masin / Pavel Macek / Tomas Wald / Lucia Motlova / Ilona Bibova / Nela Klimova / Lucie Bednarova / Vaclav Veverka / Michael Kachala / Dmitri I Svergun / Cyril Barinka / Peter Sebo / Abstract: Calcium-binding RTX proteins are equipped with C-terminal secretion signals and translocate from the Ca(2+)-depleted cytosol of Gram-negative bacteria directly into the Ca(2+)-rich external milieu, ...Calcium-binding RTX proteins are equipped with C-terminal secretion signals and translocate from the Ca(2+)-depleted cytosol of Gram-negative bacteria directly into the Ca(2+)-rich external milieu, passing through the "channel-tunnel" ducts of type I secretion systems (T1SSs). Using Bordetella pertussis adenylate cyclase toxin, we solved the structure of an essential C-terminal assembly that caps the RTX domains of RTX family leukotoxins. This is shown to scaffold directional Ca(2+)-dependent folding of the carboxy-proximal RTX repeat blocks into β-rolls. The resulting intramolecular Brownian ratchets then prevent backsliding of translocating RTX proteins in the T1SS conduits and thereby accelerate excretion of very large RTX leukotoxins from bacterial cells by a vectorial "push-ratchet" mechanism. Successive Ca(2+)-dependent and cosecretional acquisition of a functional RTX toxin structure in the course of T1SS-mediated translocation, through RTX domain folding from the C-terminal cap toward the N terminus, sets a paradigm that opens for design of virulence inhibitors of major pathogens. |
Contact author |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Data source
SASBDB page | SASDB84 |
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-Related structure data
-External links
Related items in Molecule of the Month |
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-Models
Model #485 | Type: dummy / Software: DAMMIF / Radius of dummy atoms: 1.75 A / Chi-square value: 2.128681 Search similar-shape structures of this assembly by Omokage search (details) |
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-Sample
Sample | Name: CyaA Block V / Specimen concentration: 1.30-5.00 |
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Buffer | Name: Tris HCl / Concentration: 10.00 mM / pH: 8 / Composition: 150 mM NaCl, 10 mM CaCl2 |
Entity #317 | Name: CyaA Block V / Type: protein / Description: Adenylate cyclase toxin Block V / Formula weight: 16 / Num. of mol.: 1 / Source: Bordetella pertussis / References: UniProt: P0DKX7 Sequence: Gsarddvlig daganvlngl Agndvlsgga gddvllgdeg Sdllsgdagn ddlfggqgdd tYlfgvgygh dtiyesgggh dtIrinagad qlwfarqgnd leiRilgtdd altvhdwyrd adhrveiiha anqavdqagi eklveamaqy pdp |
-Experimental information
Beam | Instrument name: PETRA III P12 / City: Hamburg / 国: Germany / Type of source: X-ray synchrotronSynchrotron / Wavelength: 0.12 Å / Dist. spec. to detc.: 3.1 mm | |||||||||||||||||||||
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Detector | Name: Pilatus 2M | |||||||||||||||||||||
Scan | Title: CyaA Block V / Measurement date: Oct 31, 2013 / Storage temperature: 10 °C / Cell temperature: 10 °C / Exposure time: 0.05 sec. / Number of frames: 20 / Unit: 1/nm /
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Distance distribution function P(R) | Sofotware P(R): GNOM 4.5a / Number of points: 389 /
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Result | D max: 5.9 / Type of curve: merged / Standard: BSA /
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