+Search query
-Structure paper
Title | The structure of the endogenous ESX-3 secretion system. |
---|---|
Journal, issue, pages | Elife, Vol. 8, Year 2019 |
Publish date | Dec 30, 2019 |
Authors | Nicole Poweleit / Nadine Czudnochowski / Rachel Nakagawa / Donovan D Trinidad / Kenan C Murphy / Christopher M Sassetti / Oren S Rosenberg / |
PubMed Abstract | 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 ...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 links | Elife / PubMed:31886769 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.7 Å |
Structure data | EMDB-20820, PDB-6umm: |
Source |
|
Keywords | TRANSPORT PROTEIN / ESX / secretion system / type VII secretion system / mycobacteria / complex / membrane protein |