Journal Article PUBDB-2017-01665

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

 ;  ;  ;  ;  ;  ;  ;  ;  ;  ;  ;  ;  ;  ;

2017
Springer Nature London

Nature microbiology 2, 17047 () [10.1038/nmicrobiol.2017.47]
 GO

This record in other databases:        

Please use a persistent id in citations: doi:  doi:

Abstract: Mycobacteria are characterized by their impermeable outer membrane, which is rich in mycolic acids$^1$. To transport substrates across this complex cell envelope, mycobacteria rely on type VII (also known as ESX) secretion systems$^2$. In Mycobacterium tuberculosis, these ESX systems are essential for growth and full virulence and therefore represent an attractive target for anti-tuberculosis drugs$^3$. However, the molecular details underlying type VII secretion are largely unknown, due to a lack of structural information. Here, we report the molecular architecture of the ESX-5 membrane complex from Mycobacterium xenopi determined at 13 Å resolution by electron microscopy. The four core proteins of the ESX-5 complex (EccB$_5$, EccC$_5$, EccD$_5$ and EccE$_5$) assemble with equimolar stoichiometry into an oligomeric assembly that displays six-fold symmetry. This membrane-associated complex seems to be embedded exclusively in the inner membrane, which indicates that additional components are required to translocate substrates across the mycobacterial outer membrane. Furthermore, the extended cytosolic domains of the EccC ATPase, which interact with secretion effectors, are highly flexible, suggesting an as yet unseen mode of substrate interaction. Comparison of our results with known structures of other bacterial secretion systems demonstrates that the architecture of type VII secretion system is fundamentally different, suggesting an alternative secretion mechanism.

Classification:

Note: © Macmillan Publishers Limited, part of Springer Nature

Contributing Institute(s):
  1. CSSB-UKE (CSSB-UKE)
  2. Centre for Structural Systems Biology (FS-CSSB-GS)
  3. EMBL (EMBL)
  4. CSSB-UKE-TM (CSSB-UKE-TM)
Research Program(s):
  1. 6215 - Soft Matter, Health and Life Sciences (POF3-621) (POF3-621)
  2. 6G3 - PETRA III (POF3-622) (POF3-622)
Experiment(s):
  1. PETRA Beamline P12 (PETRA III)

Appears in the scientific report 2017
Database coverage:
Medline ; Embargoed OpenAccess ; NCBI Molecular Biology Database
Click to display QR Code for this record

The record appears in these collections:
Private Collections > >DESY > >FS > FS-CSSB-GS
Private Collections > >CSSB > CSSB-UKE-TM
Private Collections > >CSSB > CSSB-UKE
Document types > Articles > Journal Article
Private Collections > >EMBL > EMBL
Public records
Publications database
OpenAccess

 Record created 2017-04-12, last modified 2025-07-17


Published on 2017-04-10. Available in OpenAccess from 2017-10-10.:
Download fulltext PDF
(additional files)
Rate this document:

Rate this document:
1
2
3
 
(Not yet reviewed)