Murphy, Kenan C.
Sassetti, Christopher M.
Rosenberg, Oren S.
UMass Chan AffiliationsDepartment of Microbiology and Physiological Systems
Document TypeAccepted Manuscript
Amino Acids, Peptides, and Proteins
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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 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.
Elife. 2019 Dec 30;8. pii: e52983. doi: 10.7554/eLife.52983. [Epub ahead of print] Link to article on publisher's site
Permanent Link to this Itemhttp://hdl.handle.net/20.500.14038/41305
Rights© 2019, Poweleit et al. Creative Commons Attribution 4.0 International (CC BY 4.0)
Except where otherwise noted, this item's license is described as © 2019, Poweleit et al. Creative Commons Attribution 4.0 International (CC BY 4.0)