7DHQ

Structure of Halothiobacillus neapolitanus Microcompartments Protein CsoS1D

7DHQ の概要

• エントリーDOI: 10.2210/pdb7dhq/pdb
• 分子名称: Microcompartments protein (2 entities in total)
• 機能のキーワード: microcompartments protein, csos1d, structural protein
• 由来する生物種: Halothiobacillus neapolitanus (strain ATCC 23641 / c2)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 150681.47

構造登録者

Xue, B.,Tan, Y.Q.,Ali, S.,Robinson, R.C.,Narita, A.,Yew, W.S. (登録日: 2020-11-17, 公開日: 2021-08-25, 最終更新日: 2023-11-29)

主引用文献

Tan, Y.Q.,Ali, S.,Xue, B.,Teo, W.Z.,Ling, L.H.,Go, M.K.,Lv, H.,Robinson, R.C.,Narita, A.,Yew, W.S.
Structure of a Minimal alpha-Carboxysome-Derived Shell and Its Utility in Enzyme Stabilization.
Biomacromolecules, 22:4095-4109, 2021

PubMed Abstract: Bacterial microcompartments are proteinaceous shells that encase specialized metabolic processes in bacteria. Recent advances in simplification of these intricate shells have encouraged bioengineering efforts. Here, we construct minimal shells derived from the α-carboxysome, which we term Cso-shell. Using cryogenic electron microscopy, the atomic-level structures of two shell forms were obtained, reinforcing notions of evolutionarily conserved features in bacterial microcompartment shell architecture. Encapsulation peptide sequences that facilitate loading of heterologous protein cargo within the shells were identified. We further provide a first demonstration in utilizing minimal bacterial microcompartment-derived shells for hosting heterologous enzymes. Cso-shells were found to stabilize enzymatic activities against heat shock, presence of methanol co-solvent, consecutive freeze-thawing, and alkaline environments. This study yields insights into α-carboxysome assembly and advances the utility of synthetic bacterial microcompartments as nanoreactors capable of stabilizing enzymes with varied properties and reaction chemistries.

PubMed: 34384019
DOI: 10.1021/acs.biomac.1c00533

実験手法

X-RAY DIFFRACTION (2.7 Å)