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Title: Structure and function of Mycobacterium-specific components of F-ATP synthase subunits α and ε
Authors: Bogdanović, Nebojša
Sundararaman, Lavanya
Kamariah, Neelagandan
Tyagi, Anu
Bhushan, Shashi
Ragunathan, Priya
Shin, Joon
Dick, Thomas
Grüber, Gerhard
Keywords: Science::Biological sciences::Biochemistry
Science::Biological sciences::Molecular biology
Issue Date: 2018
Source: Bogdanović, N., Sundararaman, L., Kamariah, N., Tyagi, A., Bhushan, S., Ragunathan, P., . . . Grüber, G. (2018). Structure and function of Mycobacterium-specific components of F-ATP synthase subunits α and ε. Journal of Structural Biology, 204(3), 420-434. doi:10.1016/j.jsb.2018.10.006
Journal: Journal of structural biology
Abstract: The Mycobacterium tuberculosis (Mtb) F1FO-ATP synthase (α3:β3:γ:δ:ε:a:b:b’:c9) is an essential enzyme that supplies energy for both the aerobic growing and the hypoxic dormant stage of the mycobacterial life cycle. Employing the heterologous F-ATP synthase model system αchi3:β3:γ we showed previously, that transfer of the C-terminal domain (CTD) of Mtb subunit α (Mtα514-549) to a standard F-ATP synthase α subunit suppresses ATPase activity. Here we determined the 3D reconstruction from electron micrographs of the αchi3:β3:γ complex reconstituted with the Mtb subunit ε (Mtε), which has been shown to crosstalk with the CTD of Mtα. Together with the first solution shape of Mtb subunit α (Mtα), derived from solution X-ray scattering, the structural data visualize the extended C-terminal stretch of the mycobacterial subunit α. In addition, Mtε mutants MtεR62L, MtεE87A, Mtε6-121, and Mtε1-120, reconstituted with αchi3:β3:γ provided insight into their role in coupling and in trapping inhibiting MgADP. NMR solution studies of MtεE87A gave insights into how this residue contributes to stability and crosstalk between the N-terminal domain (NTD) and the CTD of Mtε. Analyses of the N-terminal mutant Mtε6-121 highlight the differences of the NTD of mycobacterial subunit ε to the well described Geobacillus stearothermophilus or Escherichia coli counterparts. These data are discussed in context of a crosstalk between the very N-terminal amino acids of Mtε and the loop region of one c subunit of the c-ring turbine for coupling of proton-translocation and ATP synthesis activity.
ISSN: 1047-8477
DOI: 10.1016/j.jsb.2018.10.006
Rights: © 2018 Elsevier Inc. All rights reserved. This paper was published in Journal of structural biology and is made available with permission of Elsevier Inc.
Fulltext Permission: open
Fulltext Availability: With Fulltext
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