|Entry||Database: EMDB / ID: 9296|
|Title||Cryo-EM structure of the HO BMC shell: Fully asymmetric reconstruction|
|Map data||Fully asymmetric reconstruction of the HO BMC shell|
|Sample||Bacterial microcompartment shell from Haliangium ochraceum:|
|Source||Haliangium ochraceum (bacteria)|
|Method||single particle reconstruction / cryo EM / 4.4 Å resolution|
|Authors||Greber BJ / Sutter M / Kerfeld CA|
|Citation||Journal: Structure / Year: 2019|
Title: The Plasticity of Molecular Interactions Governs Bacterial Microcompartment Shell Assembly.
Authors: Basil J Greber / Markus Sutter / Cheryl A Kerfeld
Abstract: Bacterial microcompartments (BMCs) are composed of an enzymatic core encapsulated by a selectively permeable protein shell that enhances catalytic efficiency. Many pathogenic bacteria derive ...Bacterial microcompartments (BMCs) are composed of an enzymatic core encapsulated by a selectively permeable protein shell that enhances catalytic efficiency. Many pathogenic bacteria derive competitive advantages from their BMC-based catabolism, implicating BMCs as drug targets. BMC shells are of interest for bioengineering due to their diverse and selective permeability properties and because they self-assemble. A complete understanding of shell composition and organization is a prerequisite for biotechnological applications. Here, we report the cryoelectron microscopy structure of a BMC shell at 3.0-Å resolution, using an image-processing strategy that allowed us to determine the previously uncharacterized structural details of the interactions formed by the BMC-T and BMC-T shell subunits in the context of the assembled shell. We found unexpected structural plasticity among these interactions, resulting in distinct shell populations assembled from varying numbers of the BMC-T and BMC-T subunits. We discuss the implications of these findings on shell assembly and function.
|Date||Deposition: Nov 4, 2018 / Header (metadata) release: Nov 14, 2018 / Map release: Mar 13, 2019 / Last update: Mar 20, 2019|
|Structure viewer||EM map: |
Downloads & links
|File||emd_9296.map.gz (map file in CCP4 format, 536871 KB)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 1.03 Å|
CCP4 map header:
-Entire Bacterial microcompartment shell from Haliangium ochraceum
|Entire||Name: Bacterial microcompartment shell from Haliangium ochraceum|
Number of components: 1
-Component #1: cellular-component, Bacterial microcompartment shell from Haliang...
|Cellular-component||Name: Bacterial microcompartment shell from Haliangium ochraceum|
Recombinant expression: No
|Mass||Theoretical: 6.5 MDa|
|Source||Species: Haliangium ochraceum (bacteria)|
|Source (engineered)||Expression System: Escherichia coli (E. coli)|
|Specimen||Specimen state: particle / Method: cryo EM|
|Sample solution||Specimen conc.: 3 mg/ml / pH: 7.4|
|Support film||Protochips C-flat 1.2/1.3 holey carbon grids were coated with a thin carbon film and plasma cleaned using a Gatan Solarus.|
|Vitrification||Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Temperature: 277 K / Humidity: 100 %|
Details: 5-7 sec incubation of the sample on the grid before blotting and plunging.
-Electron microscopy imaging
|Imaging||Microscope: FEI TITAN|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 25 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Magnification: 48543.0 X (calibrated) / Cs: 2.7 mm / Imaging mode: BRIGHT FIELD|
|Specimen Holder||Model: GATAN LIQUID NITROGEN|
|Camera||Detector: GATAN K2 SUMMIT (4k x 4k)|
|Image acquisition||Number of digital images: 928 / Sampling size: 5 microns|
Details: 928 images retained after inspection for image quality.
|Processing||Method: single particle reconstruction / Applied symmetry: C1 (asymmetric) / Number of projections: 11107|
|3D reconstruction||Algorithm: FOURIER SPACE / Software: RELION|
CTF correction: Initial CTF fitting using CTFFIND4, CTF correction applied within RELION.
Resolution: 4.4 Å / Resolution method: FSC 0.143 CUT-OFF / Details: No symmetry applied.
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