Encapsulation mechanisms and structural studies of GRM2 bacterial microcompartment particles
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F20%3A00118308" target="_blank" >RIV/00216224:14740/20:00118308 - isvavai.cz</a>
Result on the web
<a href="https://www.nature.com/articles/s41467-019-14205-y.pdf" target="_blank" >https://www.nature.com/articles/s41467-019-14205-y.pdf</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1038/s41467-019-14205-y" target="_blank" >10.1038/s41467-019-14205-y</a>
Alternative languages
Result language
angličtina
Original language name
Encapsulation mechanisms and structural studies of GRM2 bacterial microcompartment particles
Original language description
Bacterial microcompartments (BMCs) are prokaryotic organelles consisting of a protein shell and an encapsulated enzymatic core. BMCs are involved in several biochemical processes, such as choline, glycerol and ethanolamine degradation and carbon fixation. Since non-native enzymes can also be encapsulated in BMCs, an improved understanding of BMC shell assembly and encapsulation processes could be useful for synthetic biology applications. Here we report the isolation and recombinant expression of BMC structural genes from the Klebsiella pneumoniae GRM2 locus, the investigation of mechanisms behind encapsulation of the core enzymes, and the characterization of shell particles by cryo-EM. We conclude that the enzymatic core is encapsulated in a hierarchical manner and that the CutC choline lyase may play a secondary role as an adaptor protein. We also present a cryo-EM structure of a pT=4 quasi-symmetric icosahedral shell particle at 3.3 angstrom resolution, and demonstrate variability among the minor shell forms.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
<a href="/en/project/LM2015043" target="_blank" >LM2015043: Czech Infrastructure for Integrative Structural Biology</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2020
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Nature Communications
ISSN
2041-1723
e-ISSN
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Volume of the periodical
11
Issue of the periodical within the volume
1
Country of publishing house
GB - UNITED KINGDOM
Number of pages
13
Pages from-to
388
UT code for WoS article
000512537400009
EID of the result in the Scopus database
2-s2.0-85078311746