The Plasticity of Molecular Interactions Governs Bacterial Microcompartment Shell Assembly
- Univ. of California, Berkeley, CA (United States). California Inst. for Quantitative Biosciences (QB3); Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Molecular Biophysics and Integrative Bioimaging Division
- Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Molecular Biophysics and Integrative Bioimaging Division; Michigan State Univ., East Lansing, MI (United States). MSU-DOE Plant Research Lab. and Dept. of Biochemistry and Molecular Biology
- Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Molecular Biophysics and Integrative Bioimaging Division; Michigan State Univ., East Lansing, MI (United States). MSU-DOE Plant Research Lab. and Dept. of Biochemistry and Molecula; Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Environmental Genomics and Systems Biology Division
Bacterial microcompartments (BMCs) are composed of an enzymatic core encapsulated by a selectively permeable protein shell that enhances catalytic efficiency. Many pathogenic bacteria derive competitive advantages from their BMC-based catabolism, implicating BMCs as drug targets. BMC shells are of interest for bioengineering due to their diverse and selective permeability properties and because they self-assemble. A complete understanding of shell composition and organization is a prerequisite for biotechnological applications. Here, we report the cryoelectron microscopy structure of a BMC shell at 3.0-Å resolution, using an image-processing strategy that allowed us to determine the previously uncharacterized structural details of the interactions formed by the BMC-TS and BMC-TD shell subunits in the context of the assembled shell. We found unexpected structural plasticity among these interactions, resulting in distinct shell populations assembled from varying numbers of the BMC-TS and BMC-TD subunits. We discuss the implications of these findings on shell assembly and function.
- Research Organization:
- Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States). National Energy Research Scientific Computing Center (NERSC)
- Sponsoring Organization:
- USDOE Office of Science (SC), Basic Energy Sciences (BES)
- DOE Contract Number:
- FG02-91ER20021; AC02-05CH11231
- OSTI ID:
- 1527185
- Journal Information:
- Structure, Vol. 27, Issue 5; ISSN 0969-2126
- Country of Publication:
- United States
- Language:
- English
Bio-engineering of bacterial microcompartments: a mini review
|
journal | June 2019 |
Engineering the PduT shell protein to modify the permeability of the 1,2-propanediol microcompartment of Salmonella
|
journal | December 2019 |
Functionalization of Bacterial Microcompartment Shell Proteins With Covalently Attached Heme
|
journal | January 2020 |
Similar Records
In Vitro Assembly of Diverse Bacterial Microcompartment Shell Architectures
A designed bacterial microcompartment shell with tunable composition and precision cargo loading