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6N0G

Cryo-EM structure of the HO BMC shell: subregion classified for BMC-T: TS-TDTDTD

This is a non-PDB format compatible entry.
Summary for 6N0G
Entry DOI10.2210/pdb6n0g/pdb
Related6MZU 6MZV 6MZX 6MZY 6N06 6N07 6N09 6N0F
EMDB information9296 9307 9308 9309 9310 9311 9312 9313 9314 9315
DescriptorMicrocompartments protein (3 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 chains57
Total formula weight842605.91
Authors
Greber, B.J.,Sutter, M.,Kerfeld, C.A. (deposition date: 2018-11-07, release date: 2019-03-13, Last modification date: 2024-03-20)
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 (3.6 Å)
Structure validation

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