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Title: The Plasticity of Molecular Interactions Governs Bacterial Microcompartment Shell Assembly

Journal Article · · Structure
 [1];  [2];  [3]
  1. 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
  2. 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
  3. 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

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Cited By (3)

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

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