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-Structure paper
タイトル | Priming mycobacterial ESX-secreted protein B to form a channel-like structure. |
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ジャーナル・号・ページ | Curr Res Struct Biol, Vol. 3, Page 153-164, Year 2021 |
掲載日 | 2021年6月30日 |
著者 | Abril Gijsbers / Vanesa Vinciauskaite / Axel Siroy / Ye Gao / Giancarlo Tria / Anjusha Mathew / Nuria Sánchez-Puig / Carmen López-Iglesias / Peter J Peters / Raimond B G Ravelli / |
PubMed 要旨 | 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 ...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. |
リンク | Curr Res Struct Biol / PubMed:34337436 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.29 - 2.43 Å |
構造データ | EMDB-13153, PDB-7p0z: EMDB-13154, PDB-7p13: |
由来 |
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キーワード | PROTEIN TRANSPORT / Cryo-EM / EspB / ESX-1 / Preferential orientation |