7P0Z

2.43 A Mycobacterium marinum EspB.

7P0Z の概要

• エントリーDOI: 10.2210/pdb7p0z/pdb
• EMDBエントリー: 13153
• 分子名称: ESX-1 secretion-associated protein EspB (1 entity in total)
• 機能のキーワード: cryo-em, espb, esx-1, preferential orientation, protein transport
• 由来する生物種: Mycobacterium marinum (strain ATCC BAA-535 / M)
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 218919.93

構造登録者

Gijsbers, A.,Zhang, Y.,Vinciauskaite, V.,Siroy, A.,Ye, G.,Tria, G.,Mathew, A.,Sanchez-Puig, N.,Lopez-Iglesias, C.,Peters, P.J.,Ravelli, R.B.G. (登録日: 2021-07-01, 公開日: 2021-08-18, 最終更新日: 2024-07-17)

主引用文献

Gijsbers, A.,Vinciauskaite, V.,Siroy, A.,Gao, Y.,Tria, G.,Mathew, A.,Sanchez-Puig, N.,Lopez-Iglesias, C.,Peters, P.J.,Ravelli, R.B.G.
Priming mycobacterial ESX-secreted protein B to form a channel-like structure.
Curr Res Struct Biol, 3:153-164, 2021

PubMed Abstract: ESX-1 is a major virulence factor of , a secretion machinery directly involved in the survival of the microorganism from the immune system defence. It disrupts the phagosome membrane of the host cell through a contact-dependent mechanism. Recently, the structure of the inner-membrane core complex of the homologous ESX-3 and ESX-5 was resolved; however, the elements involved in the secretion through the outer membrane or those acting on the host cell membrane are unknown. Protein substrates might form this missing element. Here, we describe the oligomerisation process of the ESX-1 substrate EspB, which occurs upon cleavage of its C-terminal region and is favoured by an acidic environment. Cryo-electron microscopy data shows that quaternary structure of EspB is conserved across slow growing species, but not in the fast growing . EspB assembles into a channel with dimensions and characteristics suitable for the transit of ESX-1 substrates, as shown by the presence of another EspB trapped within. Our results provide insight into the structure and assembly of EspB, and suggests a possible function as a structural element of ESX-1.

PubMed: 34337436
DOI: 10.1016/j.crstbi.2021.06.001

実験手法

ELECTRON MICROSCOPY (2.43 Å)