Vitamin B2 synthesis relies on a molecular lock that ensures exactly one enzyme is packed into every protein cage.
Cells manufacture complex molecules inside tiny protein shells that act like microscopic reaction chambers. For years, scientists thought these enzymes just floated into the cages at random. This discovery reveals a precise signal peptide that acts like a key to seal the cage once the correct number of parts is inside. This 1:1 ratio prevents the system from getting jammed with too many enzymes or failing due to an empty cage. Understanding this biological assembly line allows us to design custom molecular factories that never make a mistake.
A molecular basis for stoichiometric enzyme encapsulation in the vitamin B2 biosynthesis compartment
research_square · rs-8338872
Abstract Encapsulating metabolic enzymes within protein cages enhances catalytic efficiency through substrate channeling. The vitamin B2 biosynthesis system, in which a dodecahedral lumazine synthase (LS) cage encapsulates a homotrimeric riboflavin synthase (RS), exemplifies this strategy, yet the molecular basis for this stoichiometric enzyme encapsulation have remained elusive. Here, cryogenic electron microscopy structures reveal a hierarchical assembly mechanism that ensures the defined host