Simplified Alpha-Carboxysome, T=4Simplified Alpha-Carboxysome, T=4

Structural highlights

7ckc is a 240 chain structure with sequence from Halothiobacillus neapolitanus and Halothiobacillus neapolitanus c2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 2.9Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CSS4A_HALNC Probably forms vertices in the carboxysome, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, cbbL-cbbS) is sequestered. Has been modeled to induce curvature upon insertion into an otherwise flat hexagonal layer of major carboxysome subunits (Probable). A minor shell protein, only 12 pentamers of CsoS4A/CsoS4B are calculated to be present in each carboxysome. The 2 CsoS4 proteins contribute to the impermeability of the carboxysome to CO(2) (PubMed:19844578).[1] [2] Unlike beta-carboxysomes, alpha-carboxysomes (Cb) can form without cargo protein. CsoS2 is essential for Cb formation and is also capable of targeting foreign proteins to the Cb. The Cb shell assembles with the aid of CsoS2; CsoS1A, CsoS1B and CsoS1C form the majority of the shell while CsoS4A and CsoS4B form vertices. CsoS1D forms pseudohexamers that probably control metabolite flux into and out of the shell.[3]

Publication Abstract from PubMed

Bacterial microcompartments are proteinaceous shells that encase specialized metabolic processes in bacteria. Recent advances in simplification of these intricate shells have encouraged bioengineering efforts. Here, we construct minimal shells derived from the Halothiobacillus neapolitanus alpha-carboxysome, which we term Cso-shell. Using cryogenic electron microscopy, the atomic-level structures of two shell forms were obtained, reinforcing notions of evolutionarily conserved features in bacterial microcompartment shell architecture. Encapsulation peptide sequences that facilitate loading of heterologous protein cargo within the shells were identified. We further provide a first demonstration in utilizing minimal bacterial microcompartment-derived shells for hosting heterologous enzymes. Cso-shells were found to stabilize enzymatic activities against heat shock, presence of methanol co-solvent, consecutive freeze-thawing, and alkaline environments. This study yields insights into alpha-carboxysome assembly and advances the utility of synthetic bacterial microcompartments as nanoreactors capable of stabilizing enzymes with varied properties and reaction chemistries.

Structure of a Minimal alpha-Carboxysome-Derived Shell and Its Utility in Enzyme Stabilization.,Tan YQ, Ali S, Xue B, Teo WZ, Ling LH, Go MK, Lv H, Robinson RC, Narita A, Yew WS Biomacromolecules. 2021 Aug 12. doi: 10.1021/acs.biomac.1c00533. PMID:34384019[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Cai F, Menon BB, Cannon GC, Curry KJ, Shively JM, Heinhorst S. The pentameric vertex proteins are necessary for the icosahedral carboxysome shell to function as a CO2 leakage barrier. PLoS One. 2009 Oct 21;4(10):e7521. PMID:19844578 doi:10.1371/journal.pone.0007521
  2. Tanaka S, Kerfeld CA, Sawaya MR, Cai F, Heinhorst S, Cannon GC, Yeates TO. Atomic-level models of the bacterial carboxysome shell. Science. 2008 Feb 22;319(5866):1083-6. PMID:18292340 doi:http://dx.doi.org/319/5866/1083
  3. Li T, Jiang Q, Huang J, Aitchison CM, Huang F, Yang M, Dykes GF, He HL, Wang Q, Sprick RS, Cooper AI, Liu LN. Reprogramming bacterial protein organelles as a nanoreactor for hydrogen production. Nat Commun. 2020 Oct 28;11(1):5448. doi: 10.1038/s41467-020-19280-0. PMID:33116131 doi:http://dx.doi.org/10.1038/s41467-020-19280-0
  4. Tan YQ, Ali S, Xue B, Teo WZ, Ling LH, Go MK, Lv H, Robinson RC, Narita A, Yew WS. Structure of a Minimal alpha-Carboxysome-Derived Shell and Its Utility in Enzyme Stabilization. Biomacromolecules. 2021 Aug 12. doi: 10.1021/acs.biomac.1c00533. PMID:34384019 doi:http://dx.doi.org/10.1021/acs.biomac.1c00533

7ckc, resolution 2.90Å

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