Molecular interactions of the chaperone CcmS and carboxysome shell protein CcmK1 that mediate β-carboxysome assembly.

ABSTRACT: The carboxysome is a natural proteinaceous organelle for carbon fixation in cyanobacteria and chemoautotrophs. It comprises hundreds of protein homologs that self-assemble to form a polyhedral shell structure to sequester cargo enzymes, ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco), and carbonic anhydrases. How these protein components assemble to construct a functional carboxysome is a central question in not only understanding carboxysome structure and function but also synthetic engineering of carboxysomes for biotechnological applications. Here, we determined the structure of the chaperone protein CcmS, which has recently been identified to be involved in β-carboxysome assembly, and its interactions with β-carboxysome proteins. The crystal structure at 1.99 Å resolution rev

SUBMITTER: Cheng J 

PROVIDER: S-EPMC11635287 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature