6NER

Synthetic Haliangium ochraceum BMC shell

6NER の概要

• エントリーDOI: 10.2210/pdb6ner/pdb
• 分子名称: BMC-H tandem fusion protein, SULFATE ION (2 entities in total)
• 機能のキーワード: bacterial microcompartment, structural protein
• 由来する生物種: Haliangium ochraceum; 詳細
• タンパク質・核酸の鎖数: 30
• 化学式量合計: 655950.99

構造登録者

Sutter, M.,McGuire, S.,Aussignargues, C.,Kerfeld, C.A. (登録日: 2018-12-18, 公開日: 2019-04-03, 最終更新日: 2023-10-11)

主引用文献

Sutter, M.,McGuire, S.,Ferlez, B.,Kerfeld, C.A.
Structural Characterization of a Synthetic Tandem-Domain Bacterial Microcompartment Shell Protein Capable of Forming Icosahedral Shell Assemblies.
ACS Synth Biol, 8:668-674, 2019

PubMed Abstract: Bacterial microcompartments are subcellular compartments found in many prokaryotes; they consist of a protein shell that encapsulates enzymes that perform a variety of functions. The shell protects the cell from potentially toxic intermediates and colocalizes enzymes for higher efficiency. Accordingly, it is of considerable interest for biotechnological applications. We have previously structurally characterized an intact 40 nm shell comprising three different types of proteins. One of those proteins, BMC-H, forms a cyclic hexamer; here we have engineered a synthetic protein that consists of a tandem duplication of BMC-H connected by a short linker. The synthetic protein forms cyclic trimers that self-assemble to form a smaller (25 nm) icosahedral shell with gaps at the pentamer positions. When coexpressed in vivo with the pentamer fused to an affinity tag we can purify complete icosahedral shells. This engineered shell protein constitutes a minimal shell system to study permeability; reducing symmetry from 6- to 3-fold will allow for finer control of the pore environment. We have determined a crystal structure of this shell to guide rational engineering of this microcompartment shell for biotechnological applications.

PubMed: 30901520
DOI: 10.1021/acssynbio.9b00011

実験手法

X-RAY DIFFRACTION (3.59 Å)