Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural basis of light-induced redox regulation in the Calvin-Benson cycle in cyanobacteria.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 116, Issue 42, Page 20984-20990, Year 2019
Publish date	Oct 15, 2019
Authors	Ciaran R McFarlane / Nita R Shah / Burak V Kabasakal / Blanca Echeverria / Charles A R Cotton / Doryen Bubeck / James W Murray /
PubMed Abstract	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.
External links	Proc Natl Acad Sci U S A / PubMed:31570616 / PubMed Central
Methods	EM (single particle) / X-ray diffraction
Resolution	1.32 - 3.9 Å
Structure data	0071 6gve EMDB-0071, PDB-6gve: GAPDH-CP12-PRK complex Method: EM (single particle) / Resolution: 3.9 Å PDB-6gfo: cyanobacterial GAPDH with full-length CP12 Method: X-RAY DIFFRACTION / Resolution: 2.1 Å PDB-6gfp: cyanobacterial GAPDH with NADP bound Method: X-RAY DIFFRACTION / Resolution: 1.54 Å PDB-6gfq: cyanobacterial GAPDH with NAD and CP12 bound Method: X-RAY DIFFRACTION / Resolution: 1.4 Å PDB-6gfr: cyanobacterial GAPDH with NAD Method: X-RAY DIFFRACTION / Resolution: 1.919 Å PDB-6gg7: cyanobacterial GAPDH with full-length CP12 Method: X-RAY DIFFRACTION / Resolution: 1.32 Å PDB-6ghl: cyanobacterial GAPDH with full-length CP12 Method: X-RAY DIFFRACTION / Resolution: 2.378 Å PDB-6ghr: cyanobacterial GAPDH with full-length CP12 Method: X-RAY DIFFRACTION / Resolution: 2.249 Å
Chemicals	ChemComp-NAD: NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NADYM ChemComp-SO4: SULFATE ION ChemComp-HOH: WATER ChemComp-NAP: NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE ChemComp-MLI: MALONATE ION ChemComp-FMT: FORMIC ACID ChemComp-MG: Unknown entry ChemComp-ACT*: ACETATE ION
Source	thermosynechococcus elongatus bp-1 (bacteria) thermosynechococcus elongatus (strain bp-1) (bacteria) thermosynechococcus elongatus (bacteria)
Keywords	PHOTOSYNTHESIS / Calvin Cycle / Regulation / complex / redox regulation