Assembly principles and structure of a 6.5-MDa bacterial microcompartment shell
Many bacteria contain primitive organelles composed entirely of protein. These bacterial microcompartments share a common architecture of an enzymatic core encapsulated in a selectively permeable protein shell; prominent examples include the carboxysome for CO2 fixation and catabolic microcompartments found in many pathogenic microbes. The shell sequesters enzymatic reactions from the cytosol, analogous to the lipid-based membrane of eukaryotic organelles. Despite available structural information for single building blocks, the principles of shell assembly have remained elusive. Here, we present the crystal structure of an intact shell from Haliangium ochraceum, revealing the basic principles of bacterial microcompartment shell construction. Because of the conservation among shell proteins of all bacterial microcompartments, these principles apply to functionally diverse organelles and can inform the design and engineering of shells with new functionalities.
- Research Organization:
- Michigan State Univ., East Lansing, MI (United States). MSU-DOE Plant Research Laboratory; Univ. of California, Berkeley, CA (United States); Stanford Univ., CA (United States)
- Sponsoring Organization:
- USDOE Office of Science (SC), Basic Energy Sciences (BES); National Institutes of Health (NIH); Swiss National Science Foundation (SNSF)
- Grant/Contract Number:
- FG02-91ER20021; 1R01AI114975-01; AC02-05CH11231; AC02-76SF00515
- OSTI ID:
- 1434339
- Alternate ID(s):
- OSTI ID: 1596315
- Journal Information:
- Science, Journal Name: Science Vol. 356 Journal Issue: 6344; ISSN 0036-8075
- Publisher:
- AAASCopyright Statement
- Country of Publication:
- United States
- Language:
- English
Web of Science
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