Abstract
Rubisco enzymes play central roles in carbon fixation, with potential importance in biotechnology, but have eluded a full description of their multistep assembly and function. A new article describes the fascinating discovery that some archaeal Rubiscos contain a built-in assembly domain inserted into an otherwise canonical Rubisco fold, providing a tremendous expansion of our understanding of the diversity of naturally occurring Rubiscos.
Highlights
Rubisco enzymes play central roles in carbon fixation, with potential importance in biotechnology, but have eluded a full description of their multistep assembly and function
The M. burtonii Rubisco had been classified as belonging to Form II, but it contains an unusual 29-residue sequence insertion into the TIM barrel fold of the large subunits (LSU) that deviates from this form
In the ring-like L10 assemblies that are generated by the association of five dimeric (L2) subunits, each Rubisco assembly domain” (RAD) domain makes molecular contact with the adjacent LSU (Fig. 1)
Summary
Rubisco enzymes play central roles in carbon fixation, with potential importance in biotechnology, but have eluded a full description of their multistep assembly and function. Form I Rubiscos (L8S8) partner the catalytic large subunits (LSU) with small subunits (SSU) to ensure optimal activity and are known to undergo a complex folding and assembly process. Form III enzymes can function as substitutes for endogenous Rubiscos in photosynthetic bacteria [4], meaning that they offer alternative assemblies to explore Rubisco structure and function.
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