Structural Variability of EspG Chaperones from Mycobacterial ESX-1, ESX-3, and ESX-5 Type VII Secretion Systems.
Autor: | Tuukkanen AT; European Molecular Biology Laboratory, Hamburg Unit, Hamburg 22607, Germany., Freire D; European Molecular Biology Laboratory, Hamburg Unit, Hamburg 22607, Germany., Chan S; UCLA-DOE Institute, University of California Los Angeles, Los Angeles, CA 90095, USA., Arbing MA; UCLA-DOE Institute, University of California Los Angeles, Los Angeles, CA 90095, USA., Reed RW; Department of Molecular & Cellular Biochemistry, and Center for Structural Biology, University of Kentucky, Lexington, KY 40536, USA., Evans TJ; Department of Molecular & Cellular Biochemistry, and Center for Structural Biology, University of Kentucky, Lexington, KY 40536, USA., Zenkeviciutė G; European Molecular Biology Laboratory, Hamburg Unit, Hamburg 22607, Germany., Kim J; UCLA-DOE Institute, University of California Los Angeles, Los Angeles, CA 90095, USA., Kahng S; UCLA-DOE Institute, University of California Los Angeles, Los Angeles, CA 90095, USA., Sawaya MR; UCLA-DOE Institute, University of California Los Angeles, Los Angeles, CA 90095, USA., Chaton CT; Department of Molecular & Cellular Biochemistry, and Center for Structural Biology, University of Kentucky, Lexington, KY 40536, USA., Wilmanns M; European Molecular Biology Laboratory, Hamburg Unit, Hamburg 22607, Germany., Eisenberg D; UCLA-DOE Institute, University of California Los Angeles, Los Angeles, CA 90095, USA., Parret AHA; European Molecular Biology Laboratory, Hamburg Unit, Hamburg 22607, Germany. Electronic address: parret@embl-hamburg.de., Korotkov KV; Department of Molecular & Cellular Biochemistry, and Center for Structural Biology, University of Kentucky, Lexington, KY 40536, USA. Electronic address: kkorotkov@uky.edu. |
---|---|
Jazyk: | angličtina |
Zdroj: | Journal of molecular biology [J Mol Biol] 2019 Jan 18; Vol. 431 (2), pp. 289-307. Date of Electronic Publication: 2018 Nov 10. |
DOI: | 10.1016/j.jmb.2018.11.003 |
Abstrakt: | Type VII secretion systems (ESX) are responsible for transport of multiple proteins in mycobacteria. How different ESX systems achieve specific secretion of cognate substrates remains elusive. In the ESX systems, the cytoplasmic chaperone EspG forms complexes with heterodimeric PE-PPE substrates that are secreted from the cells or remain associated with the cell surface. Here we report the crystal structure of the EspG (Copyright © 2018 Elsevier Ltd. All rights reserved.) |
Databáze: | MEDLINE |
Externí odkaz: |