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

Journal Article · · Structure
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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.

Research Organization:
Michigan State Univ., East Lansing, MI (United States)
Sponsoring Organization:
USDOE Office of Science (SC), Basic Energy Sciences (BES); National Institutes of Health, National Institute of Allergy and Infectious Diseases (NIAID)
Grant/Contract Number:
FG02-91ER20021; R01 AI114975-05; AC02-05CH11231
OSTI ID:
1617538
Alternate ID(s):
OSTI ID: 1671308
Journal Information:
Structure, Journal Name: Structure Vol. 27 Journal Issue: 5; ISSN 0969-2126
Publisher:
ElsevierCopyright Statement
Country of Publication:
United Kingdom
Language:
English
Citation Metrics:
Cited by: 26 works
Citation information provided by
Web of Science

Cited By (2)

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

Figures / Tables (20)

Fig. 1(p. 23)figure Fig. 1
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Table 1(p. 37)table Table 1
Fig. S1(p. 49)figure Fig. S1
Fig. S2(p. 51)figure Fig. S2
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Fig. S8(p. 59)figure Fig. S8
Table S1 (Continued)(p. 61)table Table S1 (Continued)
Table S1(p. 62)table Table S1

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Related Subjects

59 BASIC BIOLOGICAL SCIENCES
Bacterial microcompartments
microbiology
metabolosome
modular assembly
bioengineering
structural biology
permeability
cryoelectron microscopy