Structures of EccB<sub>1</sub> and EccD<sub>1</sub> from the core complex of the mycobacterial ESX-1 type VII secretion system [electronic resource].
- Published
- Washington, D.C. : United States. Dept. of Energy. Office of Basic Energy Sciences, 2016.
Oak Ridge, Tenn. : Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy - Physical Description
- pages 1,548-1,559 : digital, PDF file
- Additional Creators
- Argonne National Laboratory, United States. Department of Energy. Office of Basic Energy Sciences, National Institutes of Health (U.S.), and United States. Department of Energy. Office of Scientific and Technical Information
Access Online
- Restrictions on Access
- Free-to-read Unrestricted online access
- Summary
- The ESX-1 type VII secretion system is an important determinant of virulence in pathogenic mycobacteria, including Mycobacterium tuberculosis. This complicated molecular machine secretes folded proteins through the mycobacterial cell envelope to subvert the host immune response. Despite its important role in disease very little is known about the molecular architecture of the ESX-1 secretion system. This study characterizes the structures of the soluble domains of two conserved core ESX-1 components – EccB1 and EccD1. The periplasmic domain of EccB1 consists of 4 repeat domains and a central domain, which together form a quasi 2-fold symmetrical structure. The repeat domains of EccB1 are structurally similar to a known peptidoglycan binding protein suggesting a role in anchoring the ESX-1 system within the periplasmic space. The cytoplasmic domain of EccD1 has a ubiquitin-like fold and forms a dimer with a negatively charged groove. In conclusion, these structures represent a major step towards resolving the molecular architecture of the entire ESX-1 assembly and may contribute to ESX-1 targeted tuberculosis intervention strategies.
- Report Numbers
- E 1.99:1249240
- Subject(s)
- Other Subject(s)
- Note
- Published through SciTech Connect.
02/27/2016.
BMC Structural Biology (Online) 16 1 ISSN 1472-6807 AM
Jonathan M. Wagner; Sum Chan; Timothy J. Evans; Sara Kahng; Jennifer Kim; Mark A. Arbing; David Eisenberg; Konstantin V. Korotkov. - Funding Information
- FC02-02ER63421
W-31-109-Eng-38.
23616-002-06 F3:02
P30GM110787
P20GM103486
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