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6MZV

Cryo-EM structure of the HO BMC shell: BMC-TD focused structure, widened inner ring

This is a non-PDB format compatible entry.
Summary for 6MZV
Entry DOI10.2210/pdb6mzv/pdb
EMDB information9308
DescriptorMicrocompartments protein (2 entities in total)
Functional Keywordsmicrocompartment, shell, compartmentalization, bmc fold, structural protein
Biological sourceHaliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2)
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Total number of polymer chains42
Total formula weight501986.67
Authors
Greber, B.J.,Sutter, M.,Kerfeld, C.A. (deposition date: 2018-11-05, release date: 2019-03-13, Last modification date: 2024-03-13)
Primary citationGreber, B.J.,Sutter, M.,Kerfeld, C.A.
The Plasticity of Molecular Interactions Governs Bacterial Microcompartment Shell Assembly.
Structure, 27:749-, 2019
Cited by
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
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.4 Å)
Structure validation

239149

數據於2025-07-23公開中

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