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 DOI | 10.2210/pdb6n0g/pdb |
Related | 6MZU 6MZV 6MZX 6MZY 6N06 6N07 6N09 6N0F |
EMDB information | 9296 9307 9308 9309 9310 9311 9312 9313 9314 9315 |
Descriptor | Microcompartments protein (3 entities in total) |
Functional Keywords | microcompartment, shell, compartmentalization, bmc fold, structural protein |
Biological source | Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2) More |
Total number of polymer chains | 57 |
Total formula weight | 842605.91 |
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 citation | Greber, 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: 30833088DOI: 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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