9BHU

Streptomyces griseus Family 2B encapsulin shell

9BHU の概要

• エントリーDOI: 10.2210/pdb9bhu/pdb
• EMDBエントリー: 44553
• 分子名称: Nucleotide-binding protein, CALCIUM ION (2 entities in total)
• 機能のキーワード: encapsulin, nanocompartment, virus like particle
• 由来する生物種: Streptomyces griseus subsp. griseus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 52054.22

構造登録者

Andreas, M.P.,Giessen, T.W. (登録日: 2024-04-22, 公開日: 2024-11-27)

主引用文献

Andreas, M.P.,Giessen, T.W.
The biosynthesis of the odorant 2-methylisoborneol is compartmentalized inside a protein shell.
Nat Commun, 15:9715-9715, 2024

PubMed Abstract: Terpenoids are the largest class of natural products, found across all domains of life. One of the most abundant bacterial terpenoids is the volatile odorant 2-methylisoborneol (2-MIB), partially responsible for the earthy smell of soil and musty taste of contaminated water. Many bacterial 2-MIB biosynthetic gene clusters were thought to encode a conserved transcription factor, named EshA in the model soil bacterium Streptomyces griseus. Here, we revise the function of EshA, now referred to as Sg Enc, and show that it is a Family 2B encapsulin shell protein. Using cryo-electron microscopy, we find that Sg Enc forms an icosahedral protein shell and encapsulates 2-methylisoborneol synthase (2-MIBS) as a cargo protein. Sg Enc contains a cyclic adenosine monophosphate (cAMP) binding domain (CBD)-fold insertion and a unique metal-binding domain, both displayed on the shell exterior. We show that Sg Enc CBDs do not bind cAMP. We find that 2-MIBS cargo loading is mediated by an N-terminal disordered cargo-loading domain and that 2-MIBS activity and Sg Enc shell structure are not modulated by cAMP. Our work redefines the function of EshA and establishes Family 2B encapsulins as cargo-loaded protein nanocompartments involved in secondary metabolite biosynthesis.

PubMed: 39521781
DOI: 10.1038/s41467-024-54175-4

実験手法

ELECTRON MICROSCOPY (2.71 Å)