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Open data
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Basic information
Entry | Database: SASBDB / ID: SASDGM5 |
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![]() | Holo-RD domain of B. Pertussis Adenylate Cyclase Toxin (CyaA)
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Function / homology | ![]() calcium- and calmodulin-responsive adenylate cyclase activity / hemolysis in another organism / adenylate cyclase / cAMP biosynthetic process / adenylate cyclase activity / channel activity / positive regulation of cytosolic calcium ion concentration / toxin activity / 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 / positive regulation of cytosolic calcium ion concentration / toxin activity / calmodulin binding / calcium ion binding / host cell plasma membrane / extracellular region / ATP binding / membrane Similarity search - Function |
Biological species | ![]() |
![]() | ![]() Title: Structural models of intrinsically disordered and calcium-bound folded states of a protein adapted for secretion. Authors: Darragh P O'Brien / Belen Hernandez / Dominique Durand / Véronique Hourdel / Ana-Cristina Sotomayor-Pérez / Patrice Vachette / Mahmoud Ghomi / Julia Chamot-Rooke / Daniel Ladant / ...Authors: Darragh P O'Brien / Belen Hernandez / Dominique Durand / Véronique Hourdel / Ana-Cristina Sotomayor-Pérez / Patrice Vachette / Mahmoud Ghomi / Julia Chamot-Rooke / Daniel Ladant / Sébastien Brier / Alexandre Chenal / ![]() Abstract: Many Gram-negative bacteria use Type I secretion systems, T1SS, to secrete virulence factors that contain calcium-binding Repeat-in-ToXin (RTX) motifs. Here, we present structural models of an RTX ...Many Gram-negative bacteria use Type I secretion systems, T1SS, to secrete virulence factors that contain calcium-binding Repeat-in-ToXin (RTX) motifs. Here, we present structural models of an RTX protein, RD, in both its intrinsically disordered calcium-free Apo-state and its folded calcium-bound Holo-state. Apo-RD behaves as a disordered polymer chain comprising several statistical elements that exhibit local rigidity with residual secondary structure. Holo-RD is a folded multi-domain protein with an anisometric shape. RTX motifs thus appear remarkably adapted to the structural and mechanistic constraints of the secretion process. In the low calcium environment of the bacterial cytosol, Apo-RD is an elongated disordered coil appropriately sized for transport through the narrow secretion machinery. The progressive folding of Holo-RD in the extracellular calcium-rich environment as it emerges form the T1SS may then favor its unidirectional export through the secretory channel. This process is relevant for hundreds of bacterial species producing virulent RTX proteins. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
-Data source
SASBDB page | ![]() |
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-Related structure data
Related structure data | C: citing same article ( |
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Similar structure data |
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External links
Related items in Molecule of the Month |
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-Models
Model #3786 | ![]() Type: atomic / Chi-square value: 1.023 / P-value: 0.000278 ![]() |
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Sample
![]() | Name: Holo-RD domain of B. Pertussis Adenylate Cyclase Toxin (CyaA) Specimen concentration: 8 mg/ml |
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Buffer | Name: 20 mM Hepes, 150 mM NaCl, 2 mM DTT, 4 mM CaCl2 / pH: 7.5 |
Entity #1895 | Name: RD domain of CyaA / Type: protein Description: RD domain of B. Pertussis Adenylate Cyclase Toxin (CyaA) Formula weight: 72.62 / Num. of mol.: 1 Source: Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251) References: UniProt: P0DKX7 Sequence: MLEHVQHIIG GAGNDSITGN AHDNFLAGGS GDDRLDGGAG NDTLVGGEGQ NTVIGGAGDD VFLQDLGVWS NQLDGGAGVD TVKYNVHQPS EERLERMGDT GIHADLQKGT VEKWPALNLF SVDHVKNIEN LHGSRLNDRI AGDDQDNELW GHDGNDTIRG RGGDDILRGG ...Sequence: MLEHVQHIIG GAGNDSITGN AHDNFLAGGS GDDRLDGGAG NDTLVGGEGQ NTVIGGAGDD VFLQDLGVWS NQLDGGAGVD TVKYNVHQPS EERLERMGDT GIHADLQKGT VEKWPALNLF SVDHVKNIEN LHGSRLNDRI AGDDQDNELW GHDGNDTIRG RGGDDILRGG LGLDTLYGED GNDIFLQDDE TVSDDIDGGA GLDTVDYSAM IHPGRIVAPH EYGFGIEADL SREWVRKASA LGVDYYDNVR NVENVIGTSM KDVLIGDAQA NTLMGQGGDD TVRGGDGDDL LFGGDGNDML YGDAGNDTLY GGLGDDTLEG GAGNDWFGQT QAREHDVLRG GDGVDTVDYS QTGAHAGIAA GRIGLGILAD LGAGRVDKLG EAGSSAYDTV SGIENVVGTE LADRITGDAQ ANVLRGAGGA DVLAGGEGDD VLLGGDGDDQ LSGDAGRDRL YGEAGDDWFF QDAANAGNLL DGGDGRDTVD FSGPGRGLDA GAKGVFLSLG KGFASLMDEP ETSNVLRNIE NAVGSARDDV LIGDAGANVL NGLAGNDVLS GGAGDDVLLG DEGSDLLSGD AGNDDLFGGQ GDDTYLFGVG YGHDTIYESG GGHDTIRINA GADQLWFARQ GNDLEIRILG TDDALTVHDW YRDADHRVEI IHAANQAVDQ AGIEKLVEAM AQYPDPGAAA AAPPAARVPD TLMQSLAVNW R |
-Experimental information
Beam | Instrument name: SOLEIL SWING ![]() ![]() | ||||||||||||||||||||||||||||||||||||||||||
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Detector | Name: AVIEX PCCD170170 / Type: CCD | ||||||||||||||||||||||||||||||||||||||||||
Scan | Measurement date: May 31, 2012 / Storage temperature: 10 °C / Cell temperature: 15 °C / Exposure time: 1 sec. / Number of frames: 250 / Unit: 1/A /
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Distance distribution function P(R) |
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Result | Comments: The scattered intensities were displayed on an absolute scale (cm-1) using the scattering of water. Frames were examined individually and 10 identical frames obtained at the end of the ...Comments: The scattered intensities were displayed on an absolute scale (cm-1) using the scattering of water. Frames were examined individually and 10 identical frames obtained at the end of the elution peak were averaged and further processed. The corresponding concentration was 0.38g/L.
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