3B20
Crystal structure of Glyceraldehyde-3-Phosphate Dehydrogenase complexed with NADfrom Synechococcus elongatus"
Summary for 3B20
| Entry DOI | 10.2210/pdb3b20/pdb |
| Descriptor | Glyceraldehyde 3-phosphate dehydrogenase (NADP+), SULFATE ION, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (4 entities in total) |
| Functional Keywords | alpha/beta fold, oxidoreductase |
| Biological source | Synechococcus elongatus |
| Total number of polymer chains | 6 |
| Total formula weight | 227325.73 |
| Authors | Matsumura, H.,Kai, A.,Maeda, T.,Inoue, T. (deposition date: 2011-07-17, release date: 2012-01-11, Last modification date: 2024-03-13) |
| Primary citation | Matsumura, H.,Kai, A.,Maeda, T.,Tamoi, M.,Satoh, A.,Tamura, H.,Hirose, M.,Ogawa, T.,Kizu, N.,Wadano, A.,Inoue, T.,Shigeoka, S. Structure Basis for the Regulation of Glyceraldehyde-3-Phosphate Dehydrogenase Activity via the Intrinsically Disordered Protein CP12. Structure, 19:1846-1854, 2011 Cited by PubMed Abstract: 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. PubMed: 22153507DOI: 10.1016/j.str.2011.08.016 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.398 Å) |
Structure validation
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