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Structure paper

タイトル	Structural basis of light-induced redox regulation in the Calvin-Benson cycle in cyanobacteria.
ジャーナル・号・ページ	Proc Natl Acad Sci U S A, Vol. 116, Issue 42, Page 20984-20990, Year 2019
掲載日	2019年10月15日
著者	Ciaran R McFarlane / Nita R Shah / Burak V Kabasakal / Blanca Echeverria / Charles A R Cotton / Doryen Bubeck / James W Murray /
PubMed 要旨	Plants, algae, and cyanobacteria fix carbon dioxide to organic carbon with the Calvin-Benson (CB) cycle. Phosphoribulokinase (PRK) and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) are essential ...Plants, algae, and cyanobacteria fix carbon dioxide to organic carbon with the Calvin-Benson (CB) cycle. Phosphoribulokinase (PRK) and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) are essential CB-cycle enzymes that control substrate availability for the carboxylation enzyme Rubisco. PRK consumes ATP to produce the Rubisco substrate ribulose bisphosphate (RuBP). GAPDH catalyzes the reduction step of the CB cycle with NADPH to produce the sugar glyceraldehyde 3-phosphate (GAP), which is used for regeneration of RuBP and is the main exit point of the cycle. GAPDH and PRK are coregulated by the redox state of a conditionally disordered protein CP12, which forms a ternary complex with both enzymes. However, the structural basis of CB-cycle regulation by CP12 is unknown. Here, we show how CP12 modulates the activity of both GAPDH and PRK. Using thermophilic cyanobacterial homologs, we solve crystal structures of GAPDH with different cofactors and CP12 bound, and the ternary GAPDH-CP12-PRK complex by electron cryo-microscopy, we reveal that formation of the N-terminal disulfide preorders CP12 prior to binding the PRK active site, which is resolved in complex with CP12. We find that CP12 binding to GAPDH influences substrate accessibility of all GAPDH active sites in the binary and ternary inhibited complexes. Our structural and biochemical data explain how CP12 integrates responses from both redox state and nicotinamide dinucleotide availability to regulate carbon fixation.
リンク	Proc Natl Acad Sci U S A / PubMed:31570616 / PubMed Central
手法	EM (単粒子) / X線回折
解像度	1.32 - 3.9 Å
構造データ	0071 6gve EMDB-0071, PDB-6gve: GAPDH-CP12-PRK complex 手法: EM (単粒子) / 解像度: 3.9 Å PDB-6gfo: cyanobacterial GAPDH with full-length CP12 手法: X-RAY DIFFRACTION / 解像度: 2.1 Å PDB-6gfp: cyanobacterial GAPDH with NADP bound 手法: X-RAY DIFFRACTION / 解像度: 1.54 Å PDB-6gfq: cyanobacterial GAPDH with NAD and CP12 bound 手法: X-RAY DIFFRACTION / 解像度: 1.4 Å PDB-6gfr: cyanobacterial GAPDH with NAD 手法: X-RAY DIFFRACTION / 解像度: 1.919 Å PDB-6gg7: cyanobacterial GAPDH with full-length CP12 手法: X-RAY DIFFRACTION / 解像度: 1.32 Å PDB-6ghl: cyanobacterial GAPDH with full-length CP12 手法: X-RAY DIFFRACTION / 解像度: 2.378 Å PDB-6ghr: cyanobacterial GAPDH with full-length CP12 手法: X-RAY DIFFRACTION / 解像度: 2.249 Å
化合物	ChemComp-NAD: NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NADYM / ニコチンアミドアデニンジヌクレオチド ChemComp-SO4: SULFATE ION / 硫酸ジアニオン / 硫酸塩 ChemComp-HOH: WATER / 水 ChemComp-NAP: NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE / ニコチンアミドアデニンジヌクレオチドリン酸 ChemComp-MLI: MALONATE ION / マロナ-ト / マロン酸 ChemComp-FMT: FORMIC ACID / ギ酸 / ギ酸 ChemComp-MG: Unknown entry / マグネシウムジカチオン ChemComp-ACT*: ACETATE ION / 酢酸イオン / 酢酸塩
由来	thermosynechococcus elongatus bp-1 (バクテリア) thermosynechococcus elongatus (strain bp-1) (バクテリア) thermosynechococcus elongatus (バクテリア)
キーワード	PHOTOSYNTHESIS (光合成) / Calvin Cycle (カルビン回路) / Regulation (規制) / complex / redox regulation