6N06

Cryo-EM structure of the HO BMC shell: BMC-T1 in the assembled shell

This is a non-PDB format compatible entry.

Summary for 6N06

• Entry DOI: 10.2210/pdb6n06/pdb
• EMDB information: 9296 9307 9308 9309 9310 9311 9312 9313
• Descriptor: Microcompartments protein (2 entities in total)
• Functional Keywords: microcompartment, shell, compartmentalization, bmc fold, structural protein
• Biological source: Haliangium ochraceum DSM 14365; More
• Total number of polymer chains: 39
• Total formula weight: 430331.45

Authors

Greber, B.J.,Sutter, M.,Kerfeld, C.A. (deposition date: 2018-11-06, release date: 2019-03-13, Last modification date: 2024-03-13)

Primary citation

Greber, B.J.,Sutter, M.,Kerfeld, C.A.
The Plasticity of Molecular Interactions Governs Bacterial Microcompartment Shell Assembly.
Structure, 27:749-, 2019

PubMed 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 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.

PubMed: 30833088
DOI: 10.1016/j.str.2019.01.017

Experimental method

ELECTRON MICROSCOPY (3.4 Å)