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TitleThe structure of the endogenous ESX-3 secretion system.
Journal, issue, pagesElife, Vol. 8, Year 2019
Publish dateDec 30, 2019
AuthorsNicole Poweleit / Nadine Czudnochowski / Rachel Nakagawa / Donovan D Trinidad / Kenan C Murphy / Christopher M Sassetti / Oren S Rosenberg /
PubMed AbstractThe ESX (or Type VII) secretion systems are protein export systems in mycobacteria and many Gram-positive bacteria that mediate a broad range of functions including virulence, conjugation, and ...The ESX (or Type VII) secretion systems are protein export systems in mycobacteria and many Gram-positive bacteria that mediate a broad range of functions including virulence, conjugation, and metabolic regulation. These systems translocate folded dimers of WXG100-superfamily protein substrates across the cytoplasmic membrane. We report the cryo-electron microscopy structure of an ESX-3 system, purified using an epitope tag inserted with recombineering into the chromosome of the model organism . The structure reveals a stacked architecture that extends above and below the inner membrane of the bacterium. The ESX-3 protomer complex is assembled from a single copy of the EccB, EccC, and EccE and two copies of the EccD protein. In the structure, the protomers form a stable dimer that is consistent with assembly into a larger oligomer. The ESX-3 structure provides a framework for further study of these important bacterial transporters.
External linksElife / PubMed:31886769 / PubMed Central
MethodsEM (single particle)
Resolution3.7 Å
Structure data

20820

6umm

EMDB-20820, PDB-6umm:
A complete structure of the ESX-3 translocon complex
Method: EM (single particle) / Resolution: 3.7 Å

Source
  • mycobacterium smegmatis (strain atcc 700084 / mc(2)155) (bacteria)
KeywordsTRANSPORT PROTEIN / ESX / secretion system / type VII secretion system / mycobacteria / complex / membrane protein

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