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-Structure paper
Title | Variety of size and form of GRM2 bacterial microcompartment particles. |
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Journal, issue, pages | Protein Sci, Vol. 30, Issue 5, Page 1035-1043, Year 2021 |
Publish date | Apr 2, 2021 |
Authors | Eva Emilija Cesle / Anatolij Filimonenko / Kaspars Tars / Gints Kalnins / |
PubMed Abstract | Bacterial microcompartments (BMCs) are bacterial organelles involved in enzymatic processes, such as carbon fixation, choline, ethanolamine and propanediol degradation, and others. Formed of a semi- ...Bacterial microcompartments (BMCs) are bacterial organelles involved in enzymatic processes, such as carbon fixation, choline, ethanolamine and propanediol degradation, and others. Formed of a semi-permeable protein shell and an enzymatic core, they can enhance enzyme performance and protect the cell from harmful intermediates. With the ability to encapsulate non-native enzymes, BMCs show high potential for applied use. For this goal, a detailed look into shell form variability is significant to predict shell adaptability. Here we present four novel 3D cryo-EM maps of recombinant Klebsiella pneumoniae GRM2 BMC shell particles with the resolution in range of 9 to 22 Å and nine novel 2D classes corresponding to discrete BMC shell forms. These structures reveal icosahedral, elongated, oblate, multi-layered and polyhedral traits of BMCs, indicating considerable variation in size and form as well as adaptability during shell formation processes. |
External links | Protein Sci / PubMed:33763934 / PubMed Central |
Methods | EM (single particle) |
Resolution | 9.0 - 22.0 Å |
Structure data | EMDB-12252: EMDB-12253: EMDB-12254: EMDB-12255: |
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