5DJB

Structure of the Haliangium ochraceum BMC-H shell protein

Summary for 5DJB

• Entry DOI: 10.2210/pdb5djb/pdb
• Related: 5DIH 5DII
• Descriptor: Microcompartments protein (2 entities in total)
• Functional Keywords: bacterial microcompartments, structural protein
• Biological source: Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2)
• Total number of polymer chains: 8
• Total formula weight: 81013.74

Authors

Sutter, M.,Kerfeld, C.A. (deposition date: 2015-09-01, release date: 2015-12-16, Last modification date: 2023-09-27)

Primary citation

Sutter, M.,Faulkner, M.,Aussignargues, C.,Paasch, B.C.,Barrett, S.,Kerfeld, C.A.,Liu, L.N.
Visualization of Bacterial Microcompartment Facet Assembly Using High-Speed Atomic Force Microscopy.
Nano Lett., 16:1590-1595, 2016

PubMed Abstract: Bacterial microcompartments (BMCs) are proteinaceous organelles widespread among bacterial phyla. They compartmentalize enzymes within a selectively permeable shell and play important roles in CO2 fixation, pathogenesis, and microbial ecology. Here, we combine X-ray crystallography and high-speed atomic force microscopy to characterize, at molecular resolution, the structure and dynamics of BMC shell facet assembly. Our results show that preformed hexamers assemble into uniformly oriented shell layers, a single hexamer thick. We also observe the dynamic process of shell facet assembly. Shell hexamers can dissociate from and incorporate into assembled sheets, indicating a flexible intermolecular interaction. Furthermore, we demonstrate that the self-assembly and dynamics of shell proteins are governed by specific contacts at the interfaces of shell proteins. Our study provides novel insights into the formation, interactions, and dynamics of BMC shell facets, which are essential for the design and engineering of self-assembled biological nanoreactors and scaffolds based on BMC architectures.

PubMed: 26617073
DOI: 10.1021/acs.nanolett.5b04259

Experimental method

X-RAY DIFFRACTION (1.798 Å)