7B9F

Structure of the mycobacterial ESX-5 Type VII Secretion System hexameric pore complex

Summary for 7B9F

• Entry DOI: 10.2210/pdb7b9f/pdb
• Related: 7B9S
• EMDB information: 12103 12105 12674
• Descriptor: EccE5, EccD5, EccC5, ... (4 entities in total)
• Functional Keywords: mycobacterial esx-5 type vii secretion system, transport protein
• Biological source: Mycobacterium xenopi RIVM700367; More
• Total number of polymer chains: 5
• Total formula weight: 357440.43

Authors

Chojnowski, G.,Ritter, C.,Beckham, K.S.H.,Mullapudi, E.,Rettel, M.,Savitski, M.M.,Mortensen, S.A.,Ziemianowicz, D.,Kosinski, J.,Wilmanns, M. (deposition date: 2020-12-14, release date: 2021-07-07, Last modification date: 2024-05-01)

Primary citation

Beckham, K.S.H.,Ritter, C.,Chojnowski, G.,Ziemianowicz, D.S.,Mullapudi, E.,Rettel, M.,Savitski, M.M.,Mortensen, S.A.,Kosinski, J.,Wilmanns, M.
Structure of the mycobacterial ESX-5 type VII secretion system pore complex.
Sci Adv, 7:-, 2021

PubMed Abstract: The ESX-5 type VII secretion system is a membrane-spanning protein complex key to the virulence of mycobacterial pathogens. However, the overall architecture of the fully assembled translocation machinery and the composition of the central secretion pore have remained unknown. Here, we present the high-resolution structure of the 2.1-megadalton ESX-5 core complex. Our structure captured a dynamic, secretion-competent conformation of the pore within a well-defined transmembrane section, sandwiched between two flexible protein layers at the cytosolic entrance and the periplasmic exit. We propose that this flexibility endows the ESX-5 machinery with large conformational plasticity required to accommodate targeted protein secretion. Compared to known secretion systems, a highly dynamic state of the pore may represent a fundamental principle of bacterial secretion machineries.

PubMed: 34172453
DOI: 10.1126/sciadv.abg9923

Experimental method

ELECTRON MICROSCOPY (3 Å)