Crystal structure of phosphoribulokinase from<i>Synechococcus</i>sp. strain PCC 6301

Wilson, Robert H.; Hayer‐Hartl, Manajit; Bracher, A.

doi:10.1107/s2053230x19002693

Cited by 17 publications

(25 citation statements)

References 43 publications

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“…The long flexible loop between residues 137–164 contains several active site residues, including Lys142, Asp146, Arg164. In a recent cyanobacterial PRK structure, it is only visible in one of the noncrystallographic dimers (7), and in our CP12-bound conformation, the loop is displaced outward relative to the crystal structure to accommodate the CP12 N-terminal domain.…”

Section: Resultsmentioning

confidence: 85%

“…In the GAPDH-CP12-PRK complex, T. elongatus PRK is dimeric, as in solution ( SI Appendix , Fig. S5 E ), and like other plant-type PRKs (6, 7). PRK has an alpha-beta-alpha sandwich fold where the central 9-strand beta-sheet is continuous across the dimer interface (Fig.…”

Section: Resultsmentioning

confidence: 91%

“…S9) and forms a disulfide with Cys41. The loop containing Cys19 is flipped to bind Cys41 in our structure and the oxidized cyanobacterial PRK structure (7), but not in the reduced PRK structures from eukaryotes (6), or the equivalent loop in the nonredox regulated archaeal PRK (26) or homologous uridine kinases (33). When this disulfide bond is oxidized in free PRK, most activity is lost (8–10).…”

Section: Resultsmentioning

confidence: 92%

“…S8). Our GAPDH-CP12 crystal structure together with models of PRK from an archaean (26) and cyanobacterium (7) were used as a basis for model building of the entire complex in Coot (27), and model refinement with Phenix (28) real space refine (Fig. 3 B and SI Appendix , Table S2).…”

Section: Resultsmentioning

confidence: 99%

“…RuBP is produced by phosphoribulokinase (PRK) in the final regeneration reaction, in which a phosphate group is transferred from ATP to ribulose 5-phosphate (5). Plant-type PRK is dimeric and has 2 conserved disulfide bonds, one at the N terminus and the other near the C terminus close to the dimer interface (6, 7). The N-terminal disulfide bond inactivates most of the activity when formed (8–10), but may be reduced in plants by thioredoxin f (11).…”

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confidence: 99%

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Structural basis of light-induced redox regulation in the Calvin–Benson cycle in cyanobacteria

McFarlane

Shah

Kabasakal

et al. 2019

Proc. Natl. Acad. Sci. U.S.A.

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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.

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Section: Resultsmentioning

confidence: 85%

Section: Resultsmentioning

confidence: 91%

Section: Resultsmentioning

confidence: 92%

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

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Structural basis of light-induced redox regulation in the Calvin–Benson cycle in cyanobacteria

McFarlane

Shah

Kabasakal

et al. 2019

Proc. Natl. Acad. Sci. U.S.A.

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Location of the photosynthetic carbon metabolism in microcompartments and separated phases in microalgal cells

Launay,

Avilan,

Gérard

et al. 2023

FEBS Letters

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Carbon acquisition, assimilation and storage in eukaryotic microalgae and cyanobacteria occur in multiple compartments that have been characterised by the location of the enzymes involved in these functions. These compartments can be delimited by bilayer membranes, such as the chloroplast, the lumen, the peroxisome, the mitochondria or monolayer membranes, such as lipid droplets or plastoglobules. They can also originate from liquid–liquid phase separation such as the pyrenoid. Multiple exchanges exist between the intracellular microcompartments, and these are reviewed for the CO2 concentration mechanism, the Calvin–Benson–Bassham cycle, the lipid metabolism and the cellular energetic balance. Progress in microscopy and spectroscopic methods opens new perspectives to characterise the molecular consequences of the location of the proteins involved, including intrinsically disordered proteins.

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