6MZX
Cryo-EM structure of the HO BMC shell: Icosahedral reconstruction (main population)
This is a non-PDB format compatible entry.
Summary for 6MZX
| Entry DOI | 10.2210/pdb6mzx/pdb |
| Related | 6MZu 6MZv 6MZY 6N06 6N07 6N09 6N0F 6N0g |
| EMDB information | 9296 9307 9308 9309 9310 9311 9312 9313 9314 9315 |
| Descriptor | Ethanolamine utilization protein EutN/carboxysome structural protein Ccml, Microcompartments protein HO-5815, Microcompartments protein HO-5816 (3 entities in total) |
| Functional Keywords | microcompartment, shell, compartmentalization, bmc fold, structural protein, virus like particle |
| Biological source | Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2) More |
| Total number of polymer chains | 9 |
| Total formula weight | 116434.90 |
| 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, 27:749-763.e4, 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 Å) |
Structure validation
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