Visualization of Bacterial Microcompartment Facet Assembly Using High-Speed Atomic Force Microscopy.

ABSTRACT: Bacterial microcompartments (BMCs) are proteinaceous organelles widespread among bacterial phyla. They compartmentalize enzymes within a selectively permeable shell and play important roles in CO2 fixation, pathogenesis, and microbial ecology. Here, we combine X-ray crystallography and high-speed atomic force microscopy to characterize, at molecular resolution, the structure and dynamics of BMC shell facet assembly. Our results show that preformed hexamers assemble into uniformly oriented shell layers, a single hexamer thick. We also observe the dynamic process of shell facet assembly. Shell hexamers can dissociate from and incorporate into assembled sheets, indicating a flexible intermolecular interaction. Furthermore, we demonstrate that the self-assembly and dynamics of shell proteins a

SUBMITTER: Sutter M 

PROVIDER: S-EPMC4789755 | biostudies-literature | 2016 Mar

REPOSITORIES: biostudies-literature