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- SASDD22: Glyceraldehyde-3-phosphate dehydrogenase in complex with oxidised... -
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Basic information
Entry | ![]() |
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![]() | Glyceraldehyde-3-phosphate dehydrogenase in complex with oxidised chloroplastic calvin cycle protein CP12 (C. reinhardtii)
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Function / homology | ![]() negative regulation of reductive pentose-phosphate cycle / supramolecular complex / Oxidoreductases; Acting on the aldehyde or oxo group of donors; With NAD+ or NADP+ as acceptor / reductive pentose-phosphate cycle / glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity / nickel cation binding / chloroplast / positive regulation of protein-containing complex assembly / glucose metabolic process / NAD binding ...negative regulation of reductive pentose-phosphate cycle / supramolecular complex / Oxidoreductases; Acting on the aldehyde or oxo group of donors; With NAD+ or NADP+ as acceptor / reductive pentose-phosphate cycle / glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity / nickel cation binding / chloroplast / positive regulation of protein-containing complex assembly / glucose metabolic process / NAD binding / NADP binding / molecular adaptor activity / lyase activity / copper ion binding / enzyme binding / protein-containing complex Similarity search - Function |
Biological species | ![]() ![]() |
![]() | ![]() 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. |
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Structure visualization
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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 | Similarity search - Function & homology ![]() |
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External links
Related items in Molecule of the Month |
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-Models
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Sample
![]() | Name: Glyceraldehyde-3-phosphate dehydrogenase in complex with oxidised chloroplastic calvin cycle protein CP12 (C. reinhardtii) Specimen concentration: 16 mg/ml / Entity id: 907 / 911 |
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Buffer | Name: 30 mM Tris, 4 mM EDTA, 100 µM NAD, 5 mM free cysteine pH: 7.9 |
Entity #907 | Name: CP12 / Type: protein / Description: Calvin cycle protein CP12, chloroplastic / Formula weight: 10.934 / Num. of mol.: 1 / Source: Chlamydomonas reinhardtii / References: UniProt: A6Q0K5 Sequence: HHHHHHHHHH SSGHIEGRHM SGQPAVDLNK KVQDAVKEAE DACAKGTSAD CAVAWDTVEE LSAAVSHKKD AVKADVTLTD PLEAFCKDAP DADECRVYED |
Entity #911 | Name: GAPDH / Type: protein / Description: Glyceraldehyde-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 ![]() ![]() | ||||||||||||||||||||||||||||||||||||
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Detector | Name: AVIEX / Type: CCD | ||||||||||||||||||||||||||||||||||||
Scan | Measurement date: Dec 8, 2010 / 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) |
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Result |
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