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

Abstract

Bacterial microcompartments (BMCs) are composed of an enzymatic core encapsulated by a selectively permeable protein shell that enhances catalytic efficiency. Many pathogenic bacteria derive a competitive advantage from their BMC based catabolism, implicating BMCs as promising 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 cryo-EM structure of a BMC shell at 3.0 32 Å resolution, using an image processing strategy that allowed us to determine the previously uncharacterized structural details of the interactions of the BMC-TS and BMC-TD shell subunits with the surrounding BMC-H 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 shell subunits. Here, our results show that heterologously produced shells are surprisingly compositonally diverse; we discuss the implications of these findings on shell assembly and function.

Authors:
; ;
Publication Date:
Research Org.:
Michigan State Univ., East Lansing, MI (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES); National Institutes of Health, National Institute of Allergy and Infectious Diseases (NIAID)
OSTI Identifier:
1617538
Alternate Identifier(s):
OSTI ID: 1671308
Grant/Contract Number:  
FG02-91ER20021; R01 AI114975-05; AC02-05CH11231
Resource Type:
Journal Article: Published Article
Journal Name:
Structure
Additional Journal Information:
Journal Name: Structure Journal Volume: 27 Journal Issue: 5; Journal ID: ISSN 0969-2126
Publisher:
Elsevier
Country of Publication:
United Kingdom
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; Bacterial microcompartments; microbiology; metabolosome; modular assembly; bioengineering; structural biology; permeability; cryoelectron microscopy

Citation Formats

Greber, Basil J., Sutter, Markus, and Kerfeld, Cheryl A. The Plasticity of Molecular Interactions Governs Bacterial Microcompartment Shell Assembly. United Kingdom: N. p., 2019. Web. doi:10.1016/j.str.2019.01.017.
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Greber, Basil J., Sutter, Markus, & Kerfeld, Cheryl A. The Plasticity of Molecular Interactions Governs Bacterial Microcompartment Shell Assembly. United Kingdom. https://doi.org/10.1016/j.str.2019.01.017
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Greber, Basil J., Sutter, Markus, and Kerfeld, Cheryl A. 2019. "The Plasticity of Molecular Interactions Governs Bacterial Microcompartment Shell Assembly". United Kingdom. https://doi.org/10.1016/j.str.2019.01.017.
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@article{osti_1617538,
title = {The Plasticity of Molecular Interactions Governs Bacterial Microcompartment Shell Assembly},
author = {Greber, Basil J. and Sutter, Markus and Kerfeld, Cheryl A.},
abstractNote = {Bacterial microcompartments (BMCs) are composed of an enzymatic core encapsulated by a selectively permeable protein shell that enhances catalytic efficiency. Many pathogenic bacteria derive a competitive advantage from their BMC based catabolism, implicating BMCs as promising 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 cryo-EM structure of a BMC shell at 3.0 32 Å resolution, using an image processing strategy that allowed us to determine the previously uncharacterized structural details of the interactions of the BMC-TS and BMC-TD shell subunits with the surrounding BMC-H 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 shell subunits. Here, our results show that heterologously produced shells are surprisingly compositonally diverse; we discuss the implications of these findings on shell assembly and function.},
doi = {10.1016/j.str.2019.01.017},
url = {https://www.osti.gov/biblio/1617538}, journal = {Structure},
issn = {0969-2126},
number = 5,
volume = 27,
place = {United Kingdom},
year = {Wed May 01 00:00:00 EDT 2019},
month = {Wed May 01 00:00:00 EDT 2019}
}
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Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record at https://doi.org/10.1016/j.str.2019.01.017
Copyright Statement
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Citation Metrics:
Cited by: 26 works
Citation information provided by
Web of Science

Figures / Tables:

Fig. 1 Fig. 1: Component structures of the HO BMC shell. (A) Cartoon representation of structures of the BMC shell proteins found in the HO shell, viewed from the side (top row) and from the top onto the concave side (bottom row; view point indicated by a blue arrow in the sidemore » view). One protein chain each is colored according to secondary structure (helix: red, sheet: yellow, first and last secondary structure elements colored darker) and marked N- and C-termini. (B) Secondary structure diagrams of the shell proteins depicted in a. BMC-H consists of a single pfam00936 domain. HO-BMC-TS1 is a member of the BMC-TS-type that comprises a fusion of two pfam00936 domains. HO-BMC-TD2 and HO-BMC-TD3 are BMC-TD-type shell proteins that are a fusion of a permuted pfam00936 domain where β4 and α3 are located at the N-terminus. BMC-P contains the all-β-sheet pfam03319 domain.« less
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Works referencing / citing this record:

Functionalization of Bacterial Microcompartment Shell Proteins With Covalently Attached Heme
journal, January 2020

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    Figures / Tables found in this record:

    Fig. 1(p. 23)figure
    Fig. 2(p. 24)figure
    Fig. 3(p. 26)figure
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    Table 1(p. 37)table
    Fig. S1(p. 49)figure
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    Fig. S8(p. 59)figure
    Table S1 (Continued)(p. 61)table
    Table S1(p. 62)table
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