Journal Article

PUBDB-2021-03825

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Structure of the mycobacterial ESX-5 type VII secretion system pore complex

Beckham, K. S. H. ; Ritter, C.CSSB*EMBL* ; Chojnowski, G. M.EMBL* ; Ziemianowicz, D.Extern* ; Mullapudi, E. ; Rettel, M. ; Savitski, M. M. ; Mortensen, S. A.EMBL* ; Kosinski, J. (Corresponding author)CSSB* ; Wilmanns, M. (Corresponding author)EMBL*

2021
Assoc. Washington, DC [u.a.]

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Please use a persistent id in citations: doi:10.1126/sciadv.abg9923  doi:10.3204/PUBDB-2021-03825

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.

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Contributing Institute(s):

1. EMBL (EMBL)
2. CSSB-EMBL (CSSB-EMBL)
3. EMBL-User (EMBL-User)
4. CSSB-EMBL-JK (CSSB-EMBL-JK)

Research Program(s):

1. 6G3 - PETRA III (DESY) (POF4-6G3) (POF4-6G3)

Experiment(s):

1. PETRA Beamline P13 (PETRA III)

Appears in the scientific report 2021

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