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-Structure paper
タイトル | Encapsulation mechanisms and structural studies of GRM2 bacterial microcompartment particles. |
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ジャーナル・号・ページ | Nat Commun, Vol. 11, Issue 1, Page 388, Year 2020 |
掲載日 | 2020年1月20日 |
著者 | Gints Kalnins / Eva-Emilija Cesle / Juris Jansons / Janis Liepins / Anatolij Filimonenko / Kaspars Tars / |
PubMed 要旨 | 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, ...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 Å resolution, and demonstrate variability among the minor shell forms. |
リンク | Nat Commun / PubMed:31959751 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.28 - 9.64 Å |
構造データ | EMDB-4595, PDB-6qn1: EMDB-4596: EMDB-4597: |
由来 |
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キーワード | STRUCTURAL PROTEIN / bacterial microcompartment / protein shell / GRM2 type microcompartment / EutN / ccmK / PduA |