5djb

Structure of the Haliangium ochraceum BMC-H shell proteinStructure of the Haliangium ochraceum BMC-H shell protein

Structural highlights

5djb is a 8 chain structure with sequence from Haliangium ochraceum DSM 14365. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.798Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BMCH_HALO1 The only hexameric shell protein in this bacterium, it forms the majority of the bacterial microcompartment (BMC) shell. Expression of 5 proteins in E.coli (BMC-H (Hoch_5815), BMC-P (Hoch_5814), and 3 BMC-T (Hoch_5812, Hoch_5816, Hoch_3341)) forms a 40 nm artificial BMC with a molecular mass of 6.5 MDa. There are 60 BMC-H hexamers per BMC. The shell facets are 20-30 Angstroms thick (a single hexamer layer), with 1 of BMC-T trimers protruding to the exterior.^[1] ^[2]

Publication Abstract from PubMed

Bacterial microcompartments (BMCs) are proteinaceous organelles widespread among bacterial phyla. They compartmentalize enzymes within a selectively permeable shell and play important roles in CO2 fixation, pathogenesis, and microbial ecology. Here, we combine X-ray crystallography and high-speed atomic force microscopy to characterize, at molecular resolution, the structure and dynamics of BMC shell facet assembly. Our results show that preformed hexamers assemble into uniformly oriented shell layers, a single hexamer thick. We also observe the dynamic process of shell facet assembly. Shell hexamers can dissociate from and incorporate into assembled sheets, indicating a flexible intermolecular interaction. Furthermore, we demonstrate that the self-assembly and dynamics of shell proteins are governed by specific contacts at the interfaces of shell proteins. Our study provides novel insights into the formation, interactions, and dynamics of BMC shell facets, which are essential for the design and engineering of self-assembled biological nanoreactors and scaffolds based on BMC architectures.

Visualization of Bacterial Microcompartment Facet Assembly Using High-Speed Atomic Force Microscopy.,Sutter M, Faulkner M, Aussignargues C, Paasch BC, Barrett S, Kerfeld CA, Liu LN Nano Lett. 2015 Dec 7. PMID:26617073^[3]

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

References

↑ Sutter M, Greber B, Aussignargues C, Kerfeld CA. Assembly principles and structure of a 6.5-MDa bacterial microcompartment shell. Science. 2017 Jun 23;356(6344):1293-1297. doi: 10.1126/science.aan3289. PMID:28642439 doi:http://dx.doi.org/10.1126/science.aan3289
↑ Greber BJ, Sutter M, Kerfeld CA. The Plasticity of Molecular Interactions Governs Bacterial Microcompartment Shell Assembly. Structure. 2019 Feb 12. pii: S0969-2126(19)30017-6. doi:, 10.1016/j.str.2019.01.017. PMID:30833088 doi:http://dx.doi.org/10.1016/j.str.2019.01.017
↑ Sutter M, Faulkner M, Aussignargues C, Paasch BC, Barrett S, Kerfeld CA, Liu LN. Visualization of Bacterial Microcompartment Facet Assembly Using High-Speed Atomic Force Microscopy. Nano Lett. 2015 Dec 7. PMID:26617073 doi:http://dx.doi.org/10.1021/acs.nanolett.5b04259

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OCA

[1] Sutter M, Greber B, Aussignargues C, Kerfeld CA. Assembly principles and structure of a 6.5-MDa bacterial microcompartment shell. Science. 2017 Jun 23;356(6344):1293-1297. doi: 10.1126/science.aan3289. PMID:28642439 doi:http://dx.doi.org/10.1126/science.aan3289

[2] Greber BJ, Sutter M, Kerfeld CA. The Plasticity of Molecular Interactions Governs Bacterial Microcompartment Shell Assembly. Structure. 2019 Feb 12. pii: S0969-2126(19)30017-6. doi:, 10.1016/j.str.2019.01.017. PMID:30833088 doi:http://dx.doi.org/10.1016/j.str.2019.01.017

[3] Sutter M, Faulkner M, Aussignargues C, Paasch BC, Barrett S, Kerfeld CA, Liu LN. Visualization of Bacterial Microcompartment Facet Assembly Using High-Speed Atomic Force Microscopy. Nano Lett. 2015 Dec 7. PMID:26617073 doi:http://dx.doi.org/10.1021/acs.nanolett.5b04259

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