+Open data
-Basic information
Entry | Database: SASBDB / ID: SASDCZ9 |
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Sample | Glyceraldehyde-3-phosphate dehydrogenase from C. reinhardtiiGlyceraldehyde 3-phosphate dehydrogenase
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Function / homology | Function and homology information Oxidoreductases; Acting on the aldehyde or oxo group of donors; With NAD+ or NADP+ as acceptor / glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity / glucose metabolic process / NAD binding / NADP binding / lyase activity Similarity search - Function |
Biological species | Chlamydomonas reinhardtii (plant) |
Citation | Journal: J Mol Biol / Year: 2018 Title: Cryptic Disorder Out of Disorder: Encounter between Conditionally Disordered CP12 and Glyceraldehyde-3-Phosphate Dehydrogenase. Authors: Hélène Launay / Patrick Barré / Carine Puppo / Yizhi Zhang / Stéphanie Maneville / Brigitte Gontero / Véronique Receveur-Bréchot / Abstract: Among intrinsically disordered proteins, conditionally disordered proteins undergo dramatic structural disorder rearrangements upon environmental changes and/or post-translational modifications that ...Among intrinsically disordered proteins, conditionally disordered proteins undergo dramatic structural disorder rearrangements upon environmental changes and/or post-translational modifications that directly modulate their function. Quantifying the dynamics of these fluctuating proteins is extremely challenging but paramount to understanding the regulation of their function. The chloroplast protein CP12 is a model of such proteins and acts as a redox switch by formation/disruption of its two disulfide bridges. It regulates the Calvin cycle by forming, in oxidized conditions, a supramolecular complex with glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and then phosphoribulokinase. In this complex, both enzymes are inactive. The highly dynamic nature of CP12 has so far hindered structural characterization explaining its mode of action. Thanks to a synergistic combination of small-angle X-ray scattering, nuclear magnetic resonance and circular dichroism that drove the molecular modeling of structural ensembles, we deciphered the structural behavior of Chlamydomonas reinhardtii oxidized CP12 alone and in the presence of GAPDH. Contrary to sequence-based structural predictions, the N-terminal region is unstable, oscillates at the ms timescale between helical and random conformations, and is connected through a disordered linker to its C-terminus, which forms a stable helical turn. Upon binding to GAPDH, oxidized CP12 undergoes an induced unfolding of its N-terminus. This phenomenon called cryptic disorder contributes to decrease the entropy cost and explains CP12 unusual high affinity for its partners. |
Contact author |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Data source
SASBDB page | SASDCZ9 |
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-Related structure data
Related structure data | C: citing same article (ref.) |
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Similar structure data |
-External links
Related items in Molecule of the Month |
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-Models
Model #1699 | Type: atomic / Radius of dummy atoms: 1.90 A / Chi-square value: 8.543929 Search similar-shape structures of this assembly by Omokage search (details) |
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Model #1700 | Type: atomic / Radius of dummy atoms: 1.90 A / Chi-square value: 8.415801 Search similar-shape structures of this assembly by Omokage search (details) |
-Sample
Sample | Name: Glyceraldehyde-3-phosphate dehydrogenase from C. reinhardtiiGlyceraldehyde 3-phosphate dehydrogenase Specimen concentration: 23 mg/ml |
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Buffer | Name: 30 mM Tris, 4 mM EDTA, 100 µM NAD, 5 mM free cysteine pH: 7.9 |
Entity #911 | Name: GAPDHGlyceraldehyde 3-phosphate dehydrogenase / Type: protein Description: Glyceraldehyde-3-phosphate dehydrogenaseGlyceraldehyde 3-phosphate dehydrogenase Formula weight: 36.881 / Num. of mol.: 4 / Source: Chlamydomonas reinhardtii / References: UniProt: A8HP84 Sequence: EKKIRVAING FGRIGRNFLR CWHGRQNTLL DVVAINDSGG VKQASHLLKY DSTLGTFAAD VKIVDDSHIS VDGKQIKIVS SRDPLQLPWK EMNIDLVIEG TGVFIDKVGA GKHIQAGASK VLITAPAKDK DIPTFVVGVN EGDYKHEYPI ISNASCTTNC LAPFVKVLEQ ...Sequence: EKKIRVAING FGRIGRNFLR CWHGRQNTLL DVVAINDSGG VKQASHLLKY DSTLGTFAAD VKIVDDSHIS VDGKQIKIVS SRDPLQLPWK EMNIDLVIEG TGVFIDKVGA GKHIQAGASK VLITAPAKDK DIPTFVVGVN EGDYKHEYPI ISNASCTTNC LAPFVKVLEQ KFGIVKGTMT TTHSYTGDQR LLDASHRDLR RARAAALNIV PTTTGAAKAV SLVLPSLKGK LNGIALRVPT PTVSVVDLVV QVEKKTFAEE VNAAFREAAN GPMKGVLHVE DAPLVSIDFK CTDQSTSIDA SLTMVMGDDM VKVVAWYDNE WGYSQRVVDL AEVTAKKWVA |
-Experimental information
Beam | Instrument name: SOLEIL SWING / City: Saint-Aubin / 国: France / Type of source: X-ray synchrotronSynchrotron / Wavelength: 0.1033 Å / Dist. spec. to detc.: 1.817 mm | ||||||||||||||||||||||||||||||||||||
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Detector | Name: AVIEX / Type: CCD | ||||||||||||||||||||||||||||||||||||
Scan | Title: Glyceraldehyde-3-phosphate dehydrogenase from C. reinhardtii Measurement date: Feb 7, 2011 / Storage temperature: 15 °C / Cell temperature: 20 °C / Exposure time: 1 sec. / Number of frames: 250 / Unit: 1/A /
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Distance distribution function P(R) | Sofotware P(R): GNOM 4.6 / Number of points: 466 /
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Result | Type of curve: sec /
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