Structure Basis for the Regulation of Glyceraldehyde-3-Phosphate Dehydrogenase Activity via the Intrinsically Disordered Protein CP12

The reversible formation of a glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-CP12-phosphoribulokinase (PRK) supramolecular complex, identified in oxygenic photosynthetic organisms, provides light-dependent Calvin cycle regulation in a coordinated manner. An intrinsically disordered protein (IDP) C...

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Bibliographic Details
Published in:Structure (London) 2011-12, Vol.19 (12), p.1846-1854
Main Authors: Matsumura, Hiroyoshi, Kai, Akihiro, Maeda, Takayuki, Tamoi, Masahiro, Satoh, Atsuko, Tamura, Haruka, Hirose, Mika, Ogawa, Taketo, Kizu, Natsuko, Wadano, Akira, Inoue, Tsuyoshi, Shigeoka, Shigeru
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Bacterial Proteins - chemistry
Bacterial Proteins - metabolism
Binding Sites
Crystallography, X-Ray
Glyceraldehyde-3-Phosphate Dehydrogenases - chemistry
Glyceraldehyde-3-Phosphate Dehydrogenases - metabolism
Molecular Sequence Data
Multiprotein Complexes - chemistry
Multiprotein Complexes - metabolism
NAD - chemistry
NAD - metabolism
Synechococcus - enzymology
Synechococcus - metabolism
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Summary:The reversible formation of a glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-CP12-phosphoribulokinase (PRK) supramolecular complex, identified in oxygenic photosynthetic organisms, provides light-dependent Calvin cycle regulation in a coordinated manner. An intrinsically disordered protein (IDP) CP12 acts as a linker to sequentially bind GAPDH and PRK to downregulate both enzymes. Here, we report the crystal structures of the ternary GAPDH-CP12-NAD and binary GAPDH-NAD complexes from Synechococcus elongates. The GAPDH-CP12 complex structure reveals that the oxidized CP12 becomes partially structured upon GAPDH binding. The C-terminus of CP12 is inserted into the active-site region of GAPDH, resulting in competitive inhibition of GAPDH. This study also provides insight into how the GAPDH-CP12 complex is dissociated by a high NADP(H)/NAD(H) ratio. An unexpected increase in negative charge potential that emerged upon CP12 binding highlights the biological function of CP12 in the sequential assembly of the supramolecular complex. ► The C-terminal region of CP12 is bound to GAPDH in complex with NAD ► The CP12 covers the substrate binding site of GAPDH ► NAD stabilizes the GAPDH-CP12 complex, but NADP does not ► An unexpected increase in negative charge potential emerges upon CP12 binding.
ISSN:0969-2126
1878-4186
DOI:10.1016/j.str.2011.08.016