Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/139321
Title: Structure and subunit arrangement of Mycobacterial F1FO ATP synthase and novel features of the unique mycobacterial subunit δ
Authors: Kamariah, Neelagandan
Huber, Roland G.
Nartey, Wilson
Bhushan, Shashi
Bond, Peter J.
Grüber, Gerhard
Keywords: Science::Biological sciences::Biochemistry
Science::Biological sciences::Molecular biology
Issue Date: 2019
Source: Kamariah, N., Huber, R. G., Nartey, W., Bhushan, S., Bond, P. J., & Grüber, G. (2019). Structure and subunit arrangement of Mycobacterial F1FO ATP synthase and novel features of the unique mycobacterial subunit δ. Journal of Structural Biology, 207(2), 199-208. doi:10.1016/j.jsb.2019.05.008
Project: NRF–CRP18–2017–01
Journal: Journal of structural biology
Abstract: In contrast to other prokaryotes, the Mycobacterial F1FO ATP synthase (α3:β3:γ:δ:ε:a:b:b’:c9) is essential for growth. The mycobacterial enzyme is also unique as a result of its 111 amino acids extended δ subunit, whose gene is fused to the peripheral stalk subunit b. Recently, the crystallographic structures of the mycobacterial α3:β3:γ:ε-domain and c subunit ring were resolved. Here, we report the first purification protocol of the intact M. smegmatis F1FO ATP synthase including the F1-domain, the entire membrane-embedded FO sector, and the stator subunits b’ and the fused b-δ. This enzyme purification enabled the determination of the first projected 2D- and 3D structure of the intact M. smegmatis F1FO ATP synthase by electron microscopy (EM) and single particle analysis. Expression and purification of the fused mycobacterial b-δ24-446 construct, excluding the membrane-embedded N-terminal amino acids, provided insight into its secondary structure. By combining these data with homology and ab-initio modeling techniques, a model of the mycobacterial peripheral stalk subunits b-δ and b’ was generated. Superposition of the 3D M. smegmatis F-ATP synthase EM-structure, the α3:β3:γ:ε and c-ring, and the derived structural models of the peripheral stalk enabled a clear assignment of all F-ATP synthase subunits, in particular with respect to the unique mycobacterial peripheral stalk subunit b’ and the elongated δ fused with subunit b. The arrangement of δ relative to the N-termini of the catalytic α3β3-headpiece and its potential as a drug target are discussed.
URI: https://hdl.handle.net/10356/139321
ISSN: 1047-8477
DOI: 10.1016/j.jsb.2019.05.008
Rights: © 2019 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
Appears in Collections:SBS Journal Articles

Files in This Item:
File Description SizeFormat 
Kamariah_etal_JSB.pdf1.32 MBAdobe PDFView/Open

SCOPUSTM   
Citations 20

15
Updated on Jan 25, 2023

Web of ScienceTM
Citations 20

15
Updated on Jan 26, 2023

Page view(s)

201
Updated on Jan 28, 2023

Download(s) 50

81
Updated on Jan 28, 2023

Google ScholarTM

Check

Altmetric


Plumx

Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.