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Secondary structure and transmembrane topology analysis of the N-terminal domain of the inner membrane protein EccE1 from M. smegmatis using site-directed spin labeling EPR.

Authors
  • Yu, Lu1
  • Fang, Wei2
  • He, Yao2
  • Cai, Wenguang3
  • Wei, Wei4
  • Tian, Changlin5
  • 1 High Magnetic Field Laboratory, Chinese Academy of Science, Hefei, Anhui 230031, China. Electronic address: [email protected] , (China)
  • 2 Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China. , (China)
  • 3 School of Life Sciences, Anhui University, 111 Jiulong Road, Hefei, Anhui 230601, China. , (China)
  • 4 Department of Chemistry, University of Science and Technology of China, Hefei 230026, China. , (China)
  • 5 High Magnetic Field Laboratory, Chinese Academy of Science, Hefei, Anhui 230031, China; Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China. Electronic address: [email protected] , (China)
Type
Published Article
Journal
Biochimica et biophysica acta. Biomembranes
Publication Date
Feb 01, 2021
Volume
1863
Issue
2
Pages
183515–183515
Identifiers
DOI: 10.1016/j.bbamem.2020.183515
PMID: 33245893
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

Protein EccE1 is an essential component of the mycobacterial ESX-1 secretion system, which plays a crucial part in the process of virulence factors secretion, especially for pathogenic mycobacteria such as Mycobacterium tuberculosis. While EccE1 was previously postulated to be the inner membrane pore-forming unit of a membrane complex through which substrates are transported, the structural properties of EccE1 remains to be explored. In the present study, systematic Site-Directed Spin Labeling (SDSL) and Electron Paramagnetic Resonance (EPR) spectroscopic studies was carried out to reveal the secondary structure and transmembrane topology of the N-terminal Domain of EccE1 protein (EccE1-NTD) from M. smegmatis in detergent micelles. EPR-based mobility and accessibility analysis of the R1 side chain for 64 residue positions of EccE1-NTD indicates that the transmembrane domain adopts two α-helices spanning Phe7-Cys30 and Leu36-Ile54. A tentative structural topology model of EccE1-NTD embedded in membrane is also suggested based on EPR spectroscopic data in this study, which will provide further insights into this protein and the ESX secretion systems of mycobacteria. Copyright © 2020 Elsevier B.V. All rights reserved.

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