Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/141945
Title: 3D reconstruction and flexibility of the hybrid engine Acetobacterium woodii F-ATP synthase
Authors: Kamariah, Neelagandan
Huber, Roland G.
Bond, Peter J.
Müller, Volker
Grüber, Gerhard
Keywords: Science::Biological sciences::Biochemistry
Issue Date: 2020
Source: Kamariah, N., Huber, R. G., Bond, P. J., Müller, V., & Grüber, G. (2020). 3D reconstruction and flexibility of the hybrid engine Acetobacterium woodii F-ATP synthase. Biochemical and Biophysical Research Communications, 527(2), 518-524. doi:10.1016/j.bbrc.2020.04.026
Journal: Biochemical and Biophysical Research Communications 
Abstract: The Na+-translocating F1FO ATP synthase from Acetobacterium woodii (AwF-ATP synthase) with a subunit stoichiometry of α3:β3:γ:δ:ε:a:b2:(c2/3)9:c1 represents an evolutionary path between ATP-synthases and vacuolar ATPases, by containing a heteromeric rotor c-ring, composed of subunits c1, c2 and c3, and an extra loop (γ195-211) within the rotary γ subunit. Here, the recombinant AwF-ATP synthase was subjected to negative stain electron microscopy and single particle analysis. The reference free 2D class averages revealed high flexibility of the enzyme, wherein the F1 and FO domains distinctively bended to adopt multiple conformations. Moreover, both the F1 and FO domains tilted relative to each other to a maximum extent of 28° and 30°, respectively. The first 3D reconstruction of the AwF-ATP synthase was determined which accommodates well the modelled structure of the AwF-ATP synthase as well as the γ195-211-loop. Molecular simulations of the enzyme underlined the bending features and flexibility observed in the electron micrographs, and enabled assessment of the dynamics of the extra γ195-211-loop.
URI: https://hdl.handle.net/10356/141945
ISSN: 0006-291X
DOI: 10.1016/j.bbrc.2020.04.026
Schools: School of Biological Sciences 
Rights: © 2020 Elsevier Inc. All rights reserved. This paper was published in Biochemical and Biophysical Research Communications and is made available with permission of Elsevier Inc.
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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