3D reconstruction and flexibility of the hybrid engine Acetobacterium woodii F-ATP synthase
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,...
| Main Authors: | , , , , |
|---|---|
| Other Authors: | |
| Format: | Journal Article |
| Language: | English |
| Published: |
2020
|
| Subjects: | |
| Online Access: | https://hdl.handle.net/10356/141945 |
| _version_ | 1811691233860386816 |
|---|---|
| author | Kamariah, Neelagandan Huber, Roland G. Bond, Peter J. Müller, Volker Grüber, Gerhard |
| author2 | School of Biological Sciences |
| author_facet | School of Biological Sciences Kamariah, Neelagandan Huber, Roland G. Bond, Peter J. Müller, Volker Grüber, Gerhard |
| author_sort | Kamariah, Neelagandan |
| collection | NTU |
| description | 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. |
| first_indexed | 2024-10-01T06:16:38Z |
| format | Journal Article |
| id | ntu-10356/141945 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T06:16:38Z |
| publishDate | 2020 |
| record_format | dspace |
| spelling | ntu-10356/1419452023-02-28T17:06:25Z 3D reconstruction and flexibility of the hybrid engine Acetobacterium woodii F-ATP synthase Kamariah, Neelagandan Huber, Roland G. Bond, Peter J. Müller, Volker Grüber, Gerhard School of Biological Sciences Science::Biological sciences::Biochemistry F-ATP synthase Na+ Transport 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. Accepted version 2020-06-12T03:10:47Z 2020-06-12T03:10:47Z 2020 Journal Article 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 0006-291X https://hdl.handle.net/10356/141945 10.1016/j.bbrc.2020.04.026 2 527 518 524 en Biochemical and Biophysical Research Communications © 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. application/pdf application/pdf |
| spellingShingle | Science::Biological sciences::Biochemistry F-ATP synthase Na+ Transport Kamariah, Neelagandan Huber, Roland G. Bond, Peter J. Müller, Volker Grüber, Gerhard 3D reconstruction and flexibility of the hybrid engine Acetobacterium woodii F-ATP synthase |
| title | 3D reconstruction and flexibility of the hybrid engine Acetobacterium woodii F-ATP synthase |
| title_full | 3D reconstruction and flexibility of the hybrid engine Acetobacterium woodii F-ATP synthase |
| title_fullStr | 3D reconstruction and flexibility of the hybrid engine Acetobacterium woodii F-ATP synthase |
| title_full_unstemmed | 3D reconstruction and flexibility of the hybrid engine Acetobacterium woodii F-ATP synthase |
| title_short | 3D reconstruction and flexibility of the hybrid engine Acetobacterium woodii F-ATP synthase |
| title_sort | 3d reconstruction and flexibility of the hybrid engine acetobacterium woodii f atp synthase |
| topic | Science::Biological sciences::Biochemistry F-ATP synthase Na+ Transport |
| url | https://hdl.handle.net/10356/141945 |
| work_keys_str_mv | AT kamariahneelagandan 3dreconstructionandflexibilityofthehybridengineacetobacteriumwoodiifatpsynthase AT huberrolandg 3dreconstructionandflexibilityofthehybridengineacetobacteriumwoodiifatpsynthase AT bondpeterj 3dreconstructionandflexibilityofthehybridengineacetobacteriumwoodiifatpsynthase AT mullervolker 3dreconstructionandflexibilityofthehybridengineacetobacteriumwoodiifatpsynthase AT grubergerhard 3dreconstructionandflexibilityofthehybridengineacetobacteriumwoodiifatpsynthase |