+Open data
-Basic information
Entry | Database: SASBDB / ID: SASDB74 |
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Sample | CyaA Block I-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 | SASDB74 |
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-Related structure data
-External links
Related items in Molecule of the Month |
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-Models
Model #484 | Type: dummy / Software: DAMMIF / Radius of dummy atoms: 4.75 A / Chi-square value: 0.839056 Search similar-shape structures of this assembly by Omokage search (details) |
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-Sample
Sample | Name: CyaA Block I-V / Specimen concentration: 1.10-4.40 |
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Buffer | Name: Tris HCl / Concentration: 10.00 mM / pH: 8 / Composition: 150 mM NaCl, 10 mM CaCl2 |
Entity #316 | Name: CyaA Block I-V / Type: protein / Description: Adenylate cyclase toxin Block I-V / Formula weight: 70 / Num. of mol.: 1 / Source: Bordetella pertussis / References: UniProt: P0DKX7 Sequence: EGDIHMSPIL GYWKIKGLVQ PTRLLLEYLE EKYEEHLYER DEGDKWRNKK FELGLEFPNL PYYIDGDVKL TQSMAIIRYI ADKHNMLGGC PKERAEISML EGAVLDIRYG VSRIAYSKDF ETLKVDFLSK LPEMLKMFED RLCHKTYLNG DHVTHPDFML YDALDVVLYM ...Sequence: EGDIHMSPIL GYWKIKGLVQ PTRLLLEYLE EKYEEHLYER DEGDKWRNKK FELGLEFPNL PYYIDGDVKL TQSMAIIRYI ADKHNMLGGC PKERAEISML EGAVLDIRYG VSRIAYSKDF ETLKVDFLSK LPEMLKMFED RLCHKTYLNG DHVTHPDFML YDALDVVLYM DPMCLDAFPK LVCFKKRIEA IPQIDKYLKS SKYIAWPLQG WQATFGGGDH PPKSDGSTSG SGHHHHHHSA GLVPRGSTAI GMKETAAAKF ERQHMDSPDL GTGGGSGIEG Renlyfqgle hvqhiiggag ndsitgnahd nflaggsgdd rldggagndt lvggegqntv iggagddvfl qdlgvwsnql dggagvdtvk ynvhqpseer lermgdtgih adlqkgtvek wpalnlfsvd hvknienlhg srlndriagd dqdnelwghd gndtirgrgg ddilrgglgl dtlygedgnd iflqddetvs ddidggagld tvdysamihp grivapheyg fgieadlsre wvrkasalgv dyydnvrnve nvigtsmkdv ligdaqantl mgqggddtvr ggdgddllfg gdgndmlygd agndtlyggl gddtleggag ndwfgqtqar ehdvlrggdg vdtvdysqtg ahagiaagri glgiladlga grvdklgeag ssaydtvsgi envvgtelad ritgdaqanv lrgaggadvl aggegddvll ggdgddqlsg dagrdrlyge agddwffqda anagnlldgg dgrdtvdfsg pgrgldagak gvflslgkgf aslmdepets nvlrnienav 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 synchrotron / Wavelength: 0.12 Å / Dist. spec. to detc.: 3.1 mm | |||||||||||||||||||||
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Detector | Name: Pilatus 2M | |||||||||||||||||||||
Scan | Title: CyaA Block I-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 4.6 / Number of points: 503 /
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Result | D max: 17.15 / Type of curve: extrapolated / Standard: BSA
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