3B1J

Crystal structure of Glyceraldehyde-3-Phosphate Dehydrogenase complexed with CP12 in the presence of copper from Synechococcus elongatus

3B1J の概要

• エントリーDOI: 10.2210/pdb3b1j/pdb
• 関連するPDBエントリー: 3B1K
• 分子名称: Glyceraldehyde 3-phosphate dehydrogenase (NADP+), CP12, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (5 entities in total)
• 機能のキーワード: alpha/beta fold, oxidoreductase-protein binding complex, oxidoreductase/protein binding
• 由来する生物種: Synechococcus elongatus; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 81179.92

構造登録者

Matsumura, H.,Kai, A.,Inoue, T. (登録日: 2011-07-04, 公開日: 2012-01-11, 最終更新日: 2024-10-23)

主引用文献

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

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: 22153507
DOI: 10.1016/j.str.2011.08.016

実験手法

X-RAY DIFFRACTION (2.2 Å)