v5.1.0.3
Cicer data from the Legume Information System
| Type | Family |
| Description | Bacterial microcompartments (BMCs) are large proteinaceous structures comprised of a roughly icosahedral shell and a series of encapsulated enzymes. They are found across bacteria where they play functionally diverse roles including CO(2) fixation and the catabolism of a range of organic compounds. They function as organelles by sequestering particular metabolic processes within the cell. A shell or capsid, which is composed of a few thousand protein subunits, surrounds a series of sequentially acting enzymes and controls the diffusion of substrates and products (including toxic or volatile intermediates) into and out of the lumen. Although functionally distinct BMCs vary in their encapsulated enzymes, all are defined by homologous shell proteins. The shells of BMCs are made primarily of a family of proteins whose structural core is the BMC domain, and variations upon this core provide functional diversity [ , , ]. This entry represents carboxysome shell protein CcmL and similar proteins from cyanobacteria. CcmL, which adopts a pentameric assembly, forms vertices in the carboxysome, a polyhedral BMC where RuBisCO (ribulose bisphosphate carboxylase) is sequestered. It induces curvature upon insertion into an otherwise flat hexagonal molecular layer of CcmK subunits ( ) [ , ]. |
| Short Name | CcmL |