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TitlePriming mycobacterial ESX-secreted protein B to form a channel-like structure.
Journal, issue, pagesCurr Res Struct Biol, Vol. 3, Page 153-164, Year 2021
Publish dateJun 30, 2021
AuthorsAbril 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 AbstractESX-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.
External linksCurr Res Struct Biol / PubMed:34337436 / PubMed Central
MethodsEM (single particle)
Resolution2.29 - 2.43 Å
Structure data

13153

7p0z

EMDB-13153, PDB-7p0z:
2.43 A Mycobacterium marinum EspB.
Method: EM (single particle) / Resolution: 2.43 Å

13154

7p13

EMDB-13154, PDB-7p13:
2.29 A Mycobacterium tuberculosis EspB.
Method: EM (single particle) / Resolution: 2.29 Å

Source
  • Mycobacterium marinum (bacteria)
  • mycobacterium marinum (strain atcc baa-535 / m) (bacteria)
  • mycobacterium tuberculosis h37rv (bacteria)
KeywordsPROTEIN TRANSPORT / Cryo-EM / EspB / ESX-1 / Preferential orientation

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