期刊
STRUCTURE
卷 19, 期 12, 页码 1846-1854出版社
CELL PRESS
DOI: 10.1016/j.str.2011.08.016
关键词
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资金
- Ministry of Education, Culture, Sports, Science and Technology of Japan [23121519, 2357104, 22550152, 22248042]
- Japan Science and Technology Agency
- Grants-in-Aid for Scientific Research [23657104, 23121519, 22550152, 22248042] Funding Source: KAKEN
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.
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