5DJB

Structure of the Haliangium ochraceum BMC-H shell protein

5DJB の概要

• エントリーDOI: 10.2210/pdb5djb/pdb
• 関連するPDBエントリー: 5DIH 5DII
• 分子名称: Microcompartments protein (2 entities in total)
• 機能のキーワード: bacterial microcompartments, structural protein
• 由来する生物種: Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2)
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 81013.74

構造登録者

Sutter, M.,Kerfeld, C.A. (登録日: 2015-09-01, 公開日: 2015-12-16, 最終更新日: 2023-09-27)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.798 Å)