Unknown

Dataset Information

0

The structure of the endogenous ESX-3 secretion system.


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 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 Mycobacterium smegmatis. 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 EccB3, EccC3, and EccE3 and two copies of the EccD3 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.

SUBMITTER: Poweleit N 

PROVIDER: S-EPMC6986878 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature

altmetric image

Publications


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 <  ...[more]

Similar Datasets

| S-EPMC8232910 | biostudies-literature
| S-EPMC4520771 | biostudies-literature
| S-EPMC4010439 | biostudies-literature
| S-EPMC7476729 | biostudies-literature
| S-EPMC3682577 | biostudies-literature
| S-EPMC7196631 | biostudies-literature
| S-EPMC4040557 | biostudies-other
| S-EPMC3927790 | biostudies-literature
| S-EPMC3272943 | biostudies-literature
| S-EPMC6331215 | biostudies-literature